ASYMMETRIC LEAVES1 (AS1, MYB91, PHAN ortholog) is a nuclear R2R3-type MYB-domain transcriptional regulator of Arabidopsis, orthologous to Antirrhinum PHANTASTICA and maize ROUGH SHEATH2. Expressed in leaf founder cells and organ primordia, AS1 heterodimerizes with the LOB-domain protein AS2 (LBD6); the AS1-AS2 complex, but neither protein alone, binds paired cis-motifs (CWGTTD and KMKTTGAHW) in the promoters of the class I KNOX genes BREVIPEDICELLUS/KNAT1 and KNAT2, and also occupies KNATM. Together with the histone deacetylase HDA6 and the histone chaperone HIRA it establishes a stable, repressive chromatin state at these loci, confining KNOX expression to the shoot apical meristem and allowing leaf determinacy and differentiation. AS1-AS2 also repress abaxial determinants (ETT/ARF3, ARF4, KAN2, YAB5) to promote adaxial leaf identity, act with auxin in leaf initiation and shape, and function as a lateral factor in fruit mediolateral patterning. Outside development, AS1 associates with CONSTANS and binds the FT promoter to promote photoperiodic flowering, damps jasmonate-dependent resistance to necrotrophic fungi while promoting defense against bacteria (an AS2-independent role), and is targeted by the geminivirus betaC1 pathogenicity protein. AS1 homodimerizes through a conserved C-terminal domain and is found in the nucleoplasm, nucleolus-associated bodies and on mitotic chromosomes.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000793 condensed chromosome | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Phylogenetic inference of activity on condensed chromosome. Reason: The IBA agrees with AS1 own observation (PMID:18713400) and the maize ortholog RS2 associating with DNA during cell division; the location is real but peripheral. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN005337045 · PTN005337045 SUPPORTS TRANSFER AS1 own IDA is among the descendant evidence. Supporting Evidence: PMID:18713400 AS1 alone was able to associate with the condensed chromosome in the metaphase cell |
| GO:0000793 condensed chromosome | IDA PMID:18713400 Subcellular localizations of AS1 and AS2 suggest their commo... | KEEP AS NON CORE | Summary: AS1 associates with condensed metaphase chromosomes. Reason: Direct observation (abstract); consistent with RS2-GFP associating with DNA during cell division (PMID:12750468) and with a role in mitotically heritable KNOX silencing, but peripheral to the core activity. Supporting Evidence: PMID:18713400 AS1 alone was able to associate with the condensed chromosome in the metaphase cell |
| GO:0000976 transcription cis-regulatory region binding | IBA GO_REF:0000033 | ACCEPT | Summary: Phylogenetic inference that AS1 binds transcription cis-regulatory regions. Reason: Consistent with experimental data on AS1 itself: the AS1-AS2 complex binds defined motifs in the BP and KNAT2 promoters (EMSA, ChIP) and AS1 occupies KNAT1, KNAT2, KNATM and FT promoters in vivo. Binding requires AS2, so in core_functions this is recorded as contributes_to. The IBA family-level placement (PTN005337045, PHAN/RS2/AS1 clade) is sound; AS1 appearing in its own With/From reflects its own experimental grounding. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN005337045 · PTN005337045 SUPPORTS TRANSFER ARS (AS1/RS2/PHAN) clade node; AS1 own ChIP/EMSA data are among the descendant evidence. Supporting Evidence: PMID:18203921 AS1 and AS2 form a repressor complex that binds directly to the regulatory motifs CWGTTD and KMKTTGAHW present at two sites in the promoters of the KNOX genes BREVIPEDICELLUS ( BP ) and KNAT2 PMID:18203921 However, when AS1 and AS2 were cotranslated, these proteins were able to bind as a complex to site X of the BP promoter PMID:23271976 Chromatin immunoprecipitation assays revealed that HDA6 and AS1 bound directly to KNAT1, KNAT2, and KNATM chromatin PMID:21950734 Moreover, AS1 bound directly to the specific regions of the FT promoter in vivo. |
| GO:0000976 transcription cis-regulatory region binding | IPI PMID:25352272 Promoter-based integration in plant defense regulation. | ACCEPT | Summary: High-throughput yeast one-hybrid hit of AS1 on a non-developmental promoter. Reason: High-throughput (e)Y1H screen in which an AS1-GAL4 activation-domain fusion activated a reporter driven by a promoter outside AS1's characterised regulon. The claim made by the term (AS1 binds transcription cis-regulatory regions) is well established for AS1 as part of the AS1-AS2 complex at KNOX promoters (ChIP, EMSA) and at the FT promoter, so the row is accepted for the term; the particular target reported here is unvalidated, and AS1 alone fails to bind DNA in EMSA, so the binding is recorded in core_functions as contributes_to. Supporting Evidence: PMID:25352272 A systematic yeast one-hybrid study was used to identify hundreds of unique potential regulatory interactions PMID:18203921 AS1 and AS2 form a repressor complex that binds directly to the regulatory motifs CWGTTD and KMKTTGAHW present at two sites in the promoters of the KNOX genes BREVIPEDICELLUS ( BP ) and KNAT2 |
| GO:0000976 transcription cis-regulatory region binding | IPI PMID:25533953 An Arabidopsis gene regulatory network for secondary cell wa... | ACCEPT | Summary: High-throughput yeast one-hybrid hit of AS1 on a non-developmental promoter. Reason: High-throughput (e)Y1H screen in which an AS1-GAL4 activation-domain fusion activated a reporter driven by a promoter outside AS1's characterised regulon. The claim made by the term (AS1 binds transcription cis-regulatory regions) is well established for AS1 as part of the AS1-AS2 complex at KNOX promoters (ChIP, EMSA) and at the FT promoter, so the row is accepted for the term; the particular target reported here is unvalidated, and AS1 alone fails to bind DNA in EMSA, so the binding is recorded in core_functions as contributes_to. Supporting Evidence: PMID:25533953 Our Y1H approach revealed a highly interconnected regulatory network. PMID:18203921 AS1 and AS2 form a repressor complex that binds directly to the regulatory motifs CWGTTD and KMKTTGAHW present at two sites in the promoters of the KNOX genes BREVIPEDICELLUS ( BP ) and KNAT2 |
| GO:0000976 transcription cis-regulatory region binding | IPI PMID:30356219 Transcriptional regulation of nitrogen-associated metabolism... | ACCEPT | Summary: High-throughput yeast one-hybrid hit of AS1 on a non-developmental promoter. Reason: High-throughput (e)Y1H screen in which an AS1-GAL4 activation-domain fusion activated a reporter driven by a promoter outside AS1's characterised regulon. The claim made by the term (AS1 binds transcription cis-regulatory regions) is well established for AS1 as part of the AS1-AS2 complex at KNOX promoters (ChIP, EMSA) and at the FT promoter, so the row is accepted for the term; the particular target reported here is unvalidated, and AS1 alone fails to bind DNA in EMSA, so the binding is recorded in core_functions as contributes_to. Supporting Evidence: PMID:30356219 Here we present a transcriptional regulatory network and twenty-one transcription factors PMID:18203921 AS1 and AS2 form a repressor complex that binds directly to the regulatory motifs CWGTTD and KMKTTGAHW present at two sites in the promoters of the KNOX genes BREVIPEDICELLUS ( BP ) and KNAT2 |
| GO:0000976 transcription cis-regulatory region binding | IPI PMID:31806676 A PXY-Mediated Transcriptional Network Integrates Signaling ... | ACCEPT | Summary: High-throughput yeast one-hybrid hit of AS1 on a non-developmental promoter. Reason: High-throughput (e)Y1H screen in which an AS1-GAL4 activation-domain fusion activated a reporter driven by a promoter outside AS1's characterised regulon. The claim made by the term (AS1 binds transcription cis-regulatory regions) is well established for AS1 as part of the AS1-AS2 complex at KNOX promoters (ChIP, EMSA) and at the FT promoter, so the row is accepted for the term; the particular target reported here is unvalidated, and AS1 alone fails to bind DNA in EMSA, so the binding is recorded in core_functions as contributes_to. Supporting Evidence: PMID:31806676 We used high-throughput enhanced yeast one-hybrid (eY1H) assays PMID:18203921 AS1 and AS2 form a repressor complex that binds directly to the regulatory motifs CWGTTD and KMKTTGAHW present at two sites in the promoters of the KNOX genes BREVIPEDICELLUS ( BP ) and KNAT2 |
| GO:0003677 DNA binding | IPI PMID:18203921 Direct repression of KNOX loci by the ASYMMETRIC LEAVES1 com... | MODIFY | Summary: DNA binding by AS1 together with AS2 (IPI, with AS2). Reason: EMSA shows that AS1 binds DNA only when co-translated with AS2 (hence the IPI with AT1G65620/AS2), and the bound sites are cis-regulatory motifs in KNOX promoters. GO:0000976 transcription cis-regulatory region binding, a descendant of DNA binding (checked with OAK) already carried by the gene, is the more precise term; AS1 contributes to this activity as part of the heterodimer. Proposed replacements: transcription cis-regulatory region binding Supporting Evidence: PMID:18203921 When translated separately, neither AS1 nor AS2 was able to bind fragment X in vitro PMID:18203921 However, when AS1 and AS2 were cotranslated, these proteins were able to bind as a complex to site X of the BP promoter PMID:18203921 AS1 and AS2 form a repressor complex that binds directly to the regulatory motifs CWGTTD and KMKTTGAHW present at two sites in the promoters of the KNOX genes BREVIPEDICELLUS ( BP ) and KNAT2 |
| GO:0003700 DNA-binding transcription factor activity | ISS PMID:11118137 Arabidopsis transcription factors: genome-wide comparative a... | ACCEPT | Summary: AS1 is a MYB-domain transcription factor. Reason: Supported by experimental data beyond the sequence similarity: the AS1-AS2 complex binds specific promoter motifs and represses KNOX genes, and AS1 binds the FT promoter. AS1 alone has a diverged R3 helix and does not bind DNA in vitro, so the activity is exerted as the AS1-AS2 heterodimer; core_functions records it as contributes_to. Supporting Evidence: PMID:11118137 Arabidopsis dedicates over 5% of its genome to code for more than 1500 transcription factors PMID:18203921 several of the amino acids in the third helix of the R3 MYB motif that are critical for MYB–DNA interaction are not conserved in AS1, and attempts to demonstrate binding of this protein to DNA in vitro have thus far been unsuccessful PMID:18203921 However, when AS1 and AS2 were cotranslated, these proteins were able to bind as a complex to site X of the BP promoter PMID:21950734 Moreover, AS1 bound directly to the specific regions of the FT promoter in vivo. |
| GO:0003700 DNA-binding transcription factor activity | ISS PMID:11882937 ASYMMETRIC LEAVES1, an Arabidopsis gene that is involved in ... | ACCEPT | Summary: AS1 is a MYB-domain transcription factor. Reason: Supported by experimental data beyond the sequence similarity: the AS1-AS2 complex binds specific promoter motifs and represses KNOX genes, and AS1 binds the FT promoter. AS1 alone has a diverged R3 helix and does not bind DNA in vitro, so the activity is exerted as the AS1-AS2 heterodimer; core_functions records it as contributes_to. Supporting Evidence: PMID:11882937 The AS1 gene encodes a MYB-domain protein that is homologous to the Antirrhinum PHANTASTICA ( PHAN) and maize ROUGH SHEATH2 ( RS2) genes. PMID:18203921 AS1 and AS2 form a repressor complex that binds directly to the regulatory motifs CWGTTD and KMKTTGAHW present at two sites in the promoters of the KNOX genes BREVIPEDICELLUS ( BP ) and KNAT2 PMID:18203921 However, when AS1 and AS2 were cotranslated, these proteins were able to bind as a complex to site X of the BP promoter PMID:21950734 Moreover, AS1 bound directly to the specific regions of the FT promoter in vivo. |
| GO:0005515 protein binding | IPI PMID:19228338 Molecular and reverse genetic characterization of NUCLEOSOME... | REMOVE | Summary: Bare protein binding from interaction data; uninformative. Reason: Per the protein-binding policy GO:0005515 is uninformative. The biologically meaningful interactions (AS2/LBD6 heterodimer, HDA6, HIRA, CO) are captured in core_functions; high-throughput Y2H partners from interactome screens are not further informative about AS1 function. Supporting Evidence: PMID:23271976 By using the BiFC assay, we found that AS1 and AS2 can interact and form homo and hetero-dimer in plant cells. |
| GO:0005515 protein binding | IPI PMID:19548978 Unequally redundant RCD1 and SRO1 mediate stress and develop... | REMOVE | Summary: Bare protein binding from interaction data; uninformative. Reason: Per the protein-binding policy GO:0005515 is uninformative. The biologically meaningful interactions (AS2/LBD6 heterodimer, HDA6, HIRA, CO) are captured in core_functions; high-throughput Y2H partners from interactome screens are not further informative about AS1 function. Supporting Evidence: PMID:23271976 By using the BiFC assay, we found that AS1 and AS2 can interact and form homo and hetero-dimer in plant cells. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: Bare protein binding from interaction data; uninformative. Reason: Per the protein-binding policy GO:0005515 is uninformative. The biologically meaningful interactions (AS2/LBD6 heterodimer, HDA6, HIRA, CO) are captured in core_functions; high-throughput Y2H partners from interactome screens are not further informative about AS1 function. Supporting Evidence: PMID:23271976 By using the BiFC assay, we found that AS1 and AS2 can interact and form homo and hetero-dimer in plant cells. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: Bare protein binding from interaction data; uninformative. Reason: Per the protein-binding policy GO:0005515 is uninformative. The biologically meaningful interactions (AS2/LBD6 heterodimer, HDA6, HIRA, CO) are captured in core_functions; high-throughput Y2H partners from interactome screens are not further informative about AS1 function. Supporting Evidence: PMID:23271976 By using the BiFC assay, we found that AS1 and AS2 can interact and form homo and hetero-dimer in plant cells. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: Bare protein binding from interaction data; uninformative. Reason: Per the protein-binding policy GO:0005515 is uninformative. The biologically meaningful interactions (AS2/LBD6 heterodimer, HDA6, HIRA, CO) are captured in core_functions; high-throughput Y2H partners from interactome screens are not further informative about AS1 function. Supporting Evidence: PMID:23271976 By using the BiFC assay, we found that AS1 and AS2 can interact and form homo and hetero-dimer in plant cells. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: Bare protein binding from interaction data; uninformative. Reason: Per the protein-binding policy GO:0005515 is uninformative. The biologically meaningful interactions (AS2/LBD6 heterodimer, HDA6, HIRA, CO) are captured in core_functions; high-throughput Y2H partners from interactome screens are not further informative about AS1 function. Supporting Evidence: PMID:23271976 By using the BiFC assay, we found that AS1 and AS2 can interact and form homo and hetero-dimer in plant cells. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: Bare protein binding from interaction data; uninformative. Reason: Per the protein-binding policy GO:0005515 is uninformative. The biologically meaningful interactions (AS2/LBD6 heterodimer, HDA6, HIRA, CO) are captured in core_functions; high-throughput Y2H partners from interactome screens are not further informative about AS1 function. Supporting Evidence: PMID:23271976 By using the BiFC assay, we found that AS1 and AS2 can interact and form homo and hetero-dimer in plant cells. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: Bare protein binding from interaction data; uninformative. Reason: Per the protein-binding policy GO:0005515 is uninformative. The biologically meaningful interactions (AS2/LBD6 heterodimer, HDA6, HIRA, CO) are captured in core_functions; high-throughput Y2H partners from interactome screens are not further informative about AS1 function. Supporting Evidence: PMID:23271976 By using the BiFC assay, we found that AS1 and AS2 can interact and form homo and hetero-dimer in plant cells. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: Bare protein binding from interaction data; uninformative. Reason: Per the protein-binding policy GO:0005515 is uninformative. The biologically meaningful interactions (AS2/LBD6 heterodimer, HDA6, HIRA, CO) are captured in core_functions; high-throughput Y2H partners from interactome screens are not further informative about AS1 function. Supporting Evidence: PMID:23271976 By using the BiFC assay, we found that AS1 and AS2 can interact and form homo and hetero-dimer in plant cells. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: Bare protein binding from interaction data; uninformative. Reason: Per the protein-binding policy GO:0005515 is uninformative. The biologically meaningful interactions (AS2/LBD6 heterodimer, HDA6, HIRA, CO) are captured in core_functions; high-throughput Y2H partners from interactome screens are not further informative about AS1 function. Supporting Evidence: PMID:23271976 By using the BiFC assay, we found that AS1 and AS2 can interact and form homo and hetero-dimer in plant cells. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: Bare protein binding from interaction data; uninformative. Reason: Per the protein-binding policy GO:0005515 is uninformative. The biologically meaningful interactions (AS2/LBD6 heterodimer, HDA6, HIRA, CO) are captured in core_functions; high-throughput Y2H partners from interactome screens are not further informative about AS1 function. Supporting Evidence: PMID:23271976 By using the BiFC assay, we found that AS1 and AS2 can interact and form homo and hetero-dimer in plant cells. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: Bare protein binding from interaction data; uninformative. Reason: Per the protein-binding policy GO:0005515 is uninformative. The biologically meaningful interactions (AS2/LBD6 heterodimer, HDA6, HIRA, CO) are captured in core_functions; high-throughput Y2H partners from interactome screens are not further informative about AS1 function. Supporting Evidence: PMID:23271976 By using the BiFC assay, we found that AS1 and AS2 can interact and form homo and hetero-dimer in plant cells. |
| GO:0005515 protein binding | IPI PMID:36088536 The protein-protein interaction landscape of transcription f... | REMOVE | Summary: Bare protein binding from interaction data; uninformative. Reason: Per the protein-binding policy GO:0005515 is uninformative. The biologically meaningful interactions (AS2/LBD6 heterodimer, HDA6, HIRA, CO) are captured in core_functions; high-throughput Y2H partners from interactome screens are not further informative about AS1 function. Supporting Evidence: PMID:23271976 By using the BiFC assay, we found that AS1 and AS2 can interact and form homo and hetero-dimer in plant cells. |
| GO:0005515 protein binding | IPI PMID:36088536 The protein-protein interaction landscape of transcription f... | REMOVE | Summary: Bare protein binding from interaction data; uninformative. Reason: Per the protein-binding policy GO:0005515 is uninformative. The biologically meaningful interactions (AS2/LBD6 heterodimer, HDA6, HIRA, CO) are captured in core_functions; high-throughput Y2H partners from interactome screens are not further informative about AS1 function. Supporting Evidence: PMID:23271976 By using the BiFC assay, we found that AS1 and AS2 can interact and form homo and hetero-dimer in plant cells. |
| GO:0005634 nucleus | EXP PMID:23271976 Histone deacetylase HDA6 is functionally associated with AS1... | ACCEPT | Summary: AS1 is nuclear (BiFC in N. benthamiana and protoplasts). Reason: Direct experimental evidence; nucleus is where AS1 acts on KNOX chromatin. Supporting Evidence: PMID:23271976 we found that HDA6 interacted with AS1 in the nucleus of as2-1 mutants PMID:23271976 Chromatin immunoprecipitation assays revealed that HDA6 and AS1 bound directly to KNAT1, KNAT2, and KNATM chromatin |
| GO:0005634 nucleus | IBA GO_REF:0000033 | ACCEPT | Summary: Phylogenetic inference of nuclear activity. Reason: Nuclear localization is shown experimentally for AS1 (BiFC with HDA6/AS2, YFP fusions) and fits its role as a chromatin-bound transcriptional repressor. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN005337045 · PTN005337045 SUPPORTS TRANSFER Supporting Evidence: PMID:23271976 we found that HDA6 interacted with AS1 in the nucleus of as2-1 mutants PMID:18713400 AS1 and AS2 alone were predominantly localized in the nucleolus and the nucleoplasm, respectively |
| GO:0005634 nucleus | IDA PMID:17293570 Histone deacetylases and ASYMMETRIC LEAVES2 are involved in ... | ACCEPT | Summary: AS1 co-localizes with AS2 in subnuclear bodies adjacent to the nucleolus. Reason: Direct localization evidence consistent with other studies. Supporting Evidence: PMID:17293570 AS2 and AS1 were colocalized in subnuclear bodies adjacent to the nucleolus |
| GO:0005634 nucleus | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt subcellular location mapping to nucleus. Reason: The UniProt location rests on experimental data (PMID:23271976) and agrees with all other localization studies. Supporting Evidence: file:ARATH/AS1/AS1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23271976}. PMID:23271976 we found that HDA6 interacted with AS1 in the nucleus of as2-1 mutants |
| GO:0005634 nucleus | ISM GO_REF:0000122 | ACCEPT | Summary: AtSubP prediction of nuclear localization. Reason: Prediction is confirmed by direct experimental localization. Supporting Evidence: PMID:23271976 we found that HDA6 interacted with AS1 in the nucleus of as2-1 mutants PMID:18713400 AS1 and AS2 alone were predominantly localized in the nucleolus and the nucleoplasm, respectively |
| GO:0005730 nucleolus | IDA PMID:18713400 Subcellular localizations of AS1 and AS2 suggest their commo... | KEEP AS NON CORE | Summary: YFP-AS1 alone is predominantly nucleolar. Reason: Direct localization (abstract read; full text not cached). Nucleolar/perinucleolar localization is reproducible (PMID:17293570) and AS1-AS2 act genetically with nucleolar factors (RH10), but the repressive activity is exerted at KNOX chromatin in the nucleoplasm, so nucleolus is kept as a non-core location. Supporting Evidence: PMID:18713400 AS1 and AS2 alone were predominantly localized in the nucleolus and the nucleoplasm, respectively PMID:17293570 AS2 and AS1 were colocalized in subnuclear bodies adjacent to the nucleolus PMID:27334696 the epigenetic repressor complex of ASYMMETRIC-LEAVES1 (AS1) and AS2 (AS1-AS2) is critical to repress abaxial (ventral) genes ETT/ARF3 and ARF4 |
| GO:0006355 regulation of DNA-templated transcription | IBA GO_REF:0000033 | MODIFY | Summary: Regulation of DNA-templated transcription. Reason: Correct but general. AS1 directly represses KNOX (BP/KNAT1, KNAT2, KNATM) and abaxial genes as part of the AS1-AS2 complex, and directly promotes FT transcription together with CONSTANS. Both negative (GO:0045892, already carried by the gene) and positive (GO:0045893) regulation of DNA-templated transcription are supported. Propagation Review Root cause: NO FAILURE CORE Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN005337045 · PTN005337045 SUPPORTS TRANSFER Family-level regulation of transcription is correct; refined to the experimentally shown directions. Proposed replacements: negative regulation of DNA-templated transcription positive regulation of DNA-templated transcription Supporting Evidence: PMID:18203921 AS1 and AS2 form a repressor complex that binds directly to the regulatory motifs CWGTTD and KMKTTGAHW present at two sites in the promoters of the KNOX genes BREVIPEDICELLUS ( BP ) and KNAT2 PMID:23271976 ASYMMETRIC LEAVES 1 (AS1) is a MYB-type transcription repressor that controls leaf development by regulating KNOX gene expression PMID:21950734 Moreover, AS1 bound directly to the specific regions of the FT promoter in vivo. |
| GO:0006355 regulation of DNA-templated transcription | IEA GO_REF:0000117 | MODIFY | Summary: Regulation of DNA-templated transcription. Reason: Correct but general. AS1 directly represses KNOX (BP/KNAT1, KNAT2, KNATM) and abaxial genes as part of the AS1-AS2 complex, and directly promotes FT transcription together with CONSTANS. Both negative (GO:0045892, already carried by the gene) and positive (GO:0045893) regulation of DNA-templated transcription are supported. Proposed replacements: negative regulation of DNA-templated transcription positive regulation of DNA-templated transcription Supporting Evidence: PMID:18203921 AS1 and AS2 form a repressor complex that binds directly to the regulatory motifs CWGTTD and KMKTTGAHW present at two sites in the promoters of the KNOX genes BREVIPEDICELLUS ( BP ) and KNAT2 PMID:23271976 ASYMMETRIC LEAVES 1 (AS1) is a MYB-type transcription repressor that controls leaf development by regulating KNOX gene expression PMID:21950734 Moreover, AS1 bound directly to the specific regions of the FT promoter in vivo. |
| GO:0008356 asymmetric cell division | IMP PMID:15608337 Asymmetric auxin response precedes asymmetric growth and dif... | MARK AS OVER ANNOTATED | Summary: as1 leaves show asymmetric auxin response and asymmetric growth. Reason: The study describes left-right asymmetry of whole as1/as2 leaves, including "asymmetry in cell division patterns" across the leaf blade. GO:0008356 asymmetric cell division is a cellular process in which one cell divides into daughters with different fates; nothing in the abstract indicates AS1 acts in such divisions. Full text not cached, so not removed. Supporting Evidence: PMID:15608337 asymmetry in cell division patterns |
| GO:0009615 response to virus | IMP PMID:18794352 betaC1, the pathogenicity factor of TYLCCNV, interacts with ... | MARK AS OVER ANNOTATED | Summary: The geminivirus betaC1 protein binds AS1 and requires it to produce disease symptoms. Reason: AS1 is the host target hijacked by the viral pathogenicity factor; the AS1-dependence of betaC1-induced leaf malformation and JA-response suppression does not show AS1 performing a response to virus. Full text not cached, so marked rather than removed. Supporting Evidence: PMID:18794352 betaC1 binds directly to AS1, elicits morphological and gene expression changes dependent on AS1 but not AS2 |
| GO:0009944 polarity specification of adaxial/abaxial axis | IMP PMID:17293570 Histone deacetylases and ASYMMETRIC LEAVES2 are involved in ... | ACCEPT | Summary: as1 enhances abaxialization when HDACs are inhibited; AS1 promotes adaxial fate. Reason: AS1-AS2 promote adaxial identity by repressing abaxial genes (ETT/ARF3, ARF4, KAN2, YAB5) and miR165/166 distribution; multiple independent genetic studies agree. A central developmental output of AS1. Supporting Evidence: PMID:17293570 Treatment of as1 or as2 plants with inhibitors of HDACs resulted in abaxialized filamentous leaves PMID:12874130 we demonstrate a new function of the AS1 and AS2 genes in the establishment of adaxial-abaxial polarity PMID:27334696 the epigenetic repressor complex of ASYMMETRIC-LEAVES1 (AS1) and AS2 (AS1-AS2) is critical to repress abaxial (ventral) genes ETT/ARF3 and ARF4 |
| GO:0009946 proximal/distal axis specification | IMP PMID:11882937 ASYMMETRIC LEAVES1, an Arabidopsis gene that is involved in ... | KEEP AS NON CORE | Summary: as1 leaves have proximodistal defects (petiole-lamina identity). Reason: Abstract describes leaf lamina with petiole-like epidermis and petiole growth beneath the lamina; supports a role upstream of proximal/distal patterning, a consequence of KNOX misexpression rather than a separate core activity. Supporting Evidence: PMID:11882937 The mutant phenotypes suggest that the ASYMMETRIC LEAVES1 ( AS1) gene is involved in the control of cell differentiation in leaves. |
| GO:0009965 leaf morphogenesis | IMP PMID:11882937 ASYMMETRIC LEAVES1, an Arabidopsis gene that is involved in ... | ACCEPT | Summary: as1 mutants have broad, lobed leaves with altered cell differentiation. Reason: Leaf morphogenesis is the defining developmental role of AS1, mediated through KNOX repression; supported by many independent studies. Supporting Evidence: PMID:11882937 The mutant phenotypes suggest that the ASYMMETRIC LEAVES1 ( AS1) gene is involved in the control of cell differentiation in leaves. PMID:11140682 AS1 negatively regulates the homeobox genes KNAT1 and KNAT2 |
| GO:0010338 leaf formation | IGI PMID:16971475 ASYMMETRIC LEAVES1 and auxin activities converge to repress ... | KEEP AS NON CORE | Summary: AS1 and auxin converge to repress BP and promote leaf fate. Reason: Genetic (IGI with PIN1, AT1G73590) evidence that AS1 acts with auxin upstream of leaf initiation; true but overlapping with leaf morphogenesis, kept as non-core. Supporting Evidence: PMID:16971475 we show that auxin and AS1 pathways converge to repress expression of the KNOX gene BREVIPEDICELLUS (BP) and thus promote leaf fate |
| GO:0042742 defense response to bacterium | IMP PMID:18003921 The developmental selector AS1 is an evolutionarily conserve... | KEEP AS NON CORE | Summary: as1 mutants are more susceptible to bacterial pathogens. Reason: AS1 is a positive regulator of SA-independent defense against bacteria, independent of AS2; real but peripheral to its developmental role. Supporting Evidence: PMID:18003921 In contrast, AS1 is a positive regulator of salicylic acid (SA)-independent extracellular defenses against bacterial pathogens. |
| GO:0042802 identical protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | MODIFY | Summary: Self-interaction of AS1 detected in high-throughput Y2H. Reason: AS1 self-association is real and is specifically a homodimer mediated by the conserved C-terminal domain; GO:0042803 protein homodimerization activity (an is_a descendant of identical protein binding, checked with OAK) is already carried by the gene and is the more precise term. Proposed replacements: protein homodimerization activity Supporting Evidence: PMID:12750468 A conserved C-terminal domain (CTD) mediates homodimerization of both RS2 and AS1 PMID:23271976 By using the BiFC assay, we found that AS1 and AS2 can interact and form homo and hetero-dimer in plant cells. |
| GO:0042802 identical protein binding | IPI PMID:36088536 The protein-protein interaction landscape of transcription f... | MODIFY | Summary: Self-interaction of AS1 detected in high-throughput Y2H. Reason: AS1 self-association is real and is specifically a homodimer mediated by the conserved C-terminal domain; GO:0042803 protein homodimerization activity (an is_a descendant of identical protein binding, checked with OAK) is already carried by the gene and is the more precise term. Proposed replacements: protein homodimerization activity Supporting Evidence: PMID:12750468 A conserved C-terminal domain (CTD) mediates homodimerization of both RS2 and AS1 PMID:23271976 By using the BiFC assay, we found that AS1 and AS2 can interact and form homo and hetero-dimer in plant cells. |
| GO:0042803 protein homodimerization activity | IPI PMID:16243907 Maize rough sheath2 and its Arabidopsis orthologue ASYMMETRI... | KEEP AS NON CORE | Summary: AS1 forms homodimers via its C-terminal domain. Reason: Homodimerization is well supported (Y2H in PMID:16243907, CTD mapping in PMID:12750468, BiFC in PMID:23271976). It is a structural property that may let AS1-AS2 complexes at two promoter sites interact, but it is not the core regulatory activity, and homodimerization is not absolutely required for KNAT1 repression. Supporting Evidence: PMID:12750468 A conserved C-terminal domain (CTD) mediates homodimerization of both RS2 and AS1 PMID:23271976 By using the BiFC assay, we found that AS1 and AS2 can interact and form homo and hetero-dimer in plant cells. PMID:16243907 RS2/AS1 can form conserved protein complexes through interaction with the DNA binding factor ASYMMETRIC LEAVES2 |
| GO:0045088 regulation of innate immune response | IMP PMID:18003921 The developmental selector AS1 is an evolutionarily conserve... | KEEP AS NON CORE | Summary: AS1 regulates inducible immune responses. Reason: AS1 dampens JA-dependent resistance to necrotrophs and promotes defense against bacteria, so regulation of innate immune response is accurate at this level; non-core. Supporting Evidence: PMID:18003921 AS1 operates as a negative regulator of inducible resistance against these pathogens by selectively binding to the promoters of genes controlled by the immune activator, jasmonic acid (JA), damping the defense response. PMID:18003921 In contrast, AS1 is a positive regulator of salicylic acid (SA)-independent extracellular defenses against bacterial pathogens. |
| GO:0045892 negative regulation of DNA-templated transcription | IDA PMID:18203921 Direct repression of KNOX loci by the ASYMMETRIC LEAVES1 com... | ACCEPT | Summary: The AS1-AS2 complex binds and represses KNOX promoters. Reason: Direct evidence: ChIP and EMSA define AS1-AS2 binding sites in BP and KNAT2 promoters and deletion of these sites derepresses BP in leaves. This is the core regulatory activity of AS1. Supporting Evidence: PMID:18203921 AS1 and AS2 form a repressor complex that binds directly to the regulatory motifs CWGTTD and KMKTTGAHW present at two sites in the promoters of the KNOX genes BREVIPEDICELLUS ( BP ) and KNAT2 PMID:23271976 Chromatin immunoprecipitation assays revealed that HDA6 and AS1 bound directly to KNAT1, KNAT2, and KNATM chromatin PMID:23271976 ASYMMETRIC LEAVES 1 (AS1) is a MYB-type transcription repressor that controls leaf development by regulating KNOX gene expression |
| GO:0050832 defense response to fungus | IMP PMID:18003921 The developmental selector AS1 is an evolutionarily conserve... | MODIFY | Summary: as1 mutants are more resistant to necrotrophic fungi. Reason: The direction is negative: loss of AS1 enhances resistance, and AS1 binds promoters of JA-controlled defense genes to damp the response. The annotation records involvement in defense response to fungus without the sign. GO has no negative regulation of defense response to fungus class (checked descendants of GO:1900150 with OAK); GO:1905035 negative regulation of antifungal innate immune response captures the finding. Proposed replacements: negative regulation of antifungal innate immune response Supporting Evidence: PMID:18003921 AS1 operates as a negative regulator of inducible resistance against these pathogens by selectively binding to the promoters of genes controlled by the immune activator, jasmonic acid (JA), damping the defense response. |
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Download this section (compressed HTML)Q: Does AS1 contact DNA directly through its diverged R2R3 MYB domain within the AS1-AS2 heterodimer (motif I, CWGTTD), with AS2 recognising motif II, or does AS2 provide all base-specific contacts?
Q: Should GO represent the AS1-AS2 heterodimer as a named transcription regulator complex so that the shared DNA-binding activity can be attributed with contributes_to to each subunit?
Q: Are the high-throughput Y1H promoter hits for AS1 (glucosinolate, secondary cell wall, nitrogen and vascular genes) bound in planta, and do they depend on AS2?
Q: Which partner (CO, or another factor) supplies DNA specificity when AS1 binds the FT promoter independently of AS2?
Experiment: Determine a structure or perform EMSA with AS1 MYB-domain point mutants (R3 helix residues) co-expressed with AS2 on motif I/II variants.
Hypothesis: Motif I is contacted by the AS1 MYB domain and motif II by the AS2 LOB domain within the heterodimer.
Type: EMSA / structural biology
Experiment: Compare AS1 ChIP-seq in wild type, as2 and co mutants in seedlings and in leaf primordia.
Hypothesis: AS1 genome-wide occupancy is largely AS2-dependent at developmental targets but AS2-independent at JA-responsive and FT promoters.
Type: ChIP-seq
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