Lsm6 is a conserved Sm-fold RNA-binding protein shared by the Lsm2-8 and Lsm1-7 complexes. Nuclear Lsm2-8 recognizes uridine-rich RNA ends and supports U6 snRNA function, spliceosome assembly and telomerase RNA protection. Cytoplasmic Lsm1-7 associates with Pat1 and promotes mRNA decapping and turnover. Fission yeast structures and RNA-binding assays establish the contribution of Lsm6 to these oligomeric RNA-binding assemblies.
Summary: mRNA splicing, via spliceosome is supported.
Reason: Lsm6 is a conserved subunit of the Lsm2-8 ring that binds U6 RNA and supports spliceosomal snRNP assembly and mRNA splicing. Fission yeast reconstitution and structures establish the target subunit within this RNA-recognition assembly.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
The multi-ORF expression system was assembled into a single plasmid through ligation independent cloning as described for Lsm2–8, with the ORFs assembled in order Lsm6, Lsm3, Lsm2, Lsm1, Lsm4, Lsm7, and Lsm5.
Summary: mRNA splicing, via spliceosome is supported.
Reason: Lsm6 is a conserved subunit of the Lsm2-8 ring that binds U6 RNA and supports spliceosomal snRNP assembly and mRNA splicing. Fission yeast reconstitution and structures establish the target subunit within this RNA-recognition assembly.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
The multi-ORF expression system was assembled into a single plasmid through ligation independent cloning as described for Lsm2–8, with the ORFs assembled in order Lsm6, Lsm3, Lsm2, Lsm1, Lsm4, Lsm7, and Lsm5.
NAS PMID:32518066 Molecular basis for the distinct cellular functions of the L...
ACCEPT
Summary: mRNA splicing, via spliceosome is supported.
Reason: Lsm6 is a conserved subunit of the Lsm2-8 ring that binds U6 RNA and supports spliceosomal snRNP assembly and mRNA splicing. Fission yeast reconstitution and structures establish the target subunit within this RNA-recognition assembly.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
The multi-ORF expression system was assembled into a single plasmid through ligation independent cloning as described for Lsm2–8, with the ORFs assembled in order Lsm6, Lsm3, Lsm2, Lsm1, Lsm4, Lsm7, and Lsm5.
Reason: Lsm6 is shared by the cytoplasmic Lsm1-7 ring, whose conserved association with Pat1 and decapping machinery underlies mRNA turnover and P-body residence. Target-specific ring reconstitution supports the complex assignment; P-body residence remains a conserved localization inference.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
The multi-ORF expression system was assembled into a single plasmid through ligation independent cloning as described for Lsm2–8, with the ORFs assembled in order Lsm6, Lsm3, Lsm2, Lsm1, Lsm4, Lsm7, and Lsm5.
Reason: Fission yeast Lsm5/6/7 subcomplex binds oligo(U) in RNA-binding assays, and intact Lsm rings reveal the RNA-recognition mechanism. This supports the subunit contribution to RNA binding without treating an isolated monomer as the physiological RNA-binding species.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
The multi-ORF expression system was assembled into a single plasmid through ligation independent cloning as described for Lsm2–8, with the ORFs assembled in order Lsm6, Lsm3, Lsm2, Lsm1, Lsm4, Lsm7, and Lsm5.
Reason: Fission yeast Lsm5/6/7 subcomplex binds oligo(U) in RNA-binding assays, and intact Lsm rings reveal the RNA-recognition mechanism. This supports the subunit contribution to RNA binding without treating an isolated monomer as the physiological RNA-binding species.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
The multi-ORF expression system was assembled into a single plasmid through ligation independent cloning as described for Lsm2–8, with the ORFs assembled in order Lsm6, Lsm3, Lsm2, Lsm1, Lsm4, Lsm7, and Lsm5.
IPI PMID:22615807 Crystal structures of Lsm3, Lsm4 and Lsm5/6/7 from Schizosac...
KEEP AS NON CORE
Summary: protein binding is retained as an ancillary annotation.
Reason: Retain the reported physical interaction as supporting complex-assembly evidence. Generic protein binding does not specify the nuclease or RNA-binding function and is not a useful core molecular-function summary.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
IPI PMID:22615807 Crystal structures of Lsm3, Lsm4 and Lsm5/6/7 from Schizosac...
KEEP AS NON CORE
Summary: protein binding is retained as an ancillary annotation.
Reason: Retain the reported physical interaction as supporting complex-assembly evidence. Generic protein binding does not specify the nuclease or RNA-binding function and is not a useful core molecular-function summary.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ...
ACCEPT
Summary: nucleus is supported.
Reason: The nuclear pool is consistent with the localization screen and the Lsm2-8 role in U6 RNA metabolism. ARBA agreement is not the basis of acceptance.
Next, we determined the localization of 4,431 proteins, corresponding to approximately 90% of the fission yeast proteome, by tagging each ORF with the yellow fluorescent protein.
The multi-ORF expression system was assembled into a single plasmid through ligation independent cloning as described for Lsm2–8, with the ORFs assembled in order Lsm6, Lsm3, Lsm2, Lsm1, Lsm4, Lsm7, and Lsm5.
Reason: The nuclear pool is consistent with the localization screen and the Lsm2-8 role in U6 RNA metabolism. ARBA agreement is not the basis of acceptance.
Next, we determined the localization of 4,431 proteins, corresponding to approximately 90% of the fission yeast proteome, by tagging each ORF with the yellow fluorescent protein.
The multi-ORF expression system was assembled into a single plasmid through ligation independent cloning as described for Lsm2–8, with the ORFs assembled in order Lsm6, Lsm3, Lsm2, Lsm1, Lsm4, Lsm7, and Lsm5.
IDA PMID:26292707 Structure of a yeast spliceosome at 3.6-angstrom resolution.
UNDECIDED
Summary: U5 snRNP is not fully resolved.
Reason: The accessible main text of PMID:26292707 describes Sm rings associated with U2 and U5, while fission yeast Lsm6 is experimentally established in Lsm RNA-binding rings. The exact protein identities and contacts underlying the PomBase U2/U5 assignment require resolution against the supplementary models and chain mappings. The broader spliceosome context is compatible with Lsm6 function, but it does not by itself settle this precise RNA or particle assignment.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
EXP PMID:26292707 Structure of a yeast spliceosome at 3.6-angstrom resolution.
UNDECIDED
Summary: U2 snRNP is not fully resolved.
Reason: The accessible main text of PMID:26292707 describes Sm rings associated with U2 and U5, while fission yeast Lsm6 is experimentally established in Lsm RNA-binding rings. The exact protein identities and contacts underlying the PomBase U2/U5 assignment require resolution against the supplementary models and chain mappings. The broader spliceosome context is compatible with Lsm6 function, but it does not by itself settle this precise RNA or particle assignment.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
EXP PMID:32518066 Molecular basis for the distinct cellular functions of the L...
ACCEPT
Summary: U6 snRNP is supported.
Reason: Lsm6 is a conserved subunit of the Lsm2-8 ring that binds U6 RNA and supports spliceosomal snRNP assembly and mRNA splicing. Fission yeast reconstitution and structures establish the target subunit within this RNA-recognition assembly.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
The multi-ORF expression system was assembled into a single plasmid through ligation independent cloning as described for Lsm2–8, with the ORFs assembled in order Lsm6, Lsm3, Lsm2, Lsm1, Lsm4, Lsm7, and Lsm5.
Reason: Lsm6 is a conserved subunit of the Lsm2-8 ring that binds U6 RNA and supports spliceosomal snRNP assembly and mRNA splicing. Fission yeast reconstitution and structures establish the target subunit within this RNA-recognition assembly.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
The multi-ORF expression system was assembled into a single plasmid through ligation independent cloning as described for Lsm2–8, with the ORFs assembled in order Lsm6, Lsm3, Lsm2, Lsm1, Lsm4, Lsm7, and Lsm5.
EXP PMID:35277511 The methyl phosphate capping enzyme Bmc1/Bin3 is a stable co...
ACCEPT
Summary: telomerase holoenzyme complex is supported.
Reason: The nuclear Lsm2-8 ring protects telomerase RNA and supports telomerase assembly in fission yeast. This is a complex-level RNA-stabilization role, not reverse-transcriptase catalysis. The target is an experimentally established shared Lsm2-8 subunit. The original PMID:35277511 annotation is retained at its stated evidential scope; accessible source text and the independent evidence cited here are considered together.
The multi-ORF expression system was assembled into a single plasmid through ligation independent cloning as described for Lsm2–8, with the ORFs assembled in order Lsm6, Lsm3, Lsm2, Lsm1, Lsm4, Lsm7, and Lsm5.
Co-immunoprecipitation assays confirmed an interaction between Lsm3 and Lar7 (Fig. 5b), indicating that they co-exist as a complex. Their association was sensitive to the presence of RNase and was abolished in lar7-W103A and lar7-FV197EE mutants. In addition, an interaction between wild-type Lar7 and Trt1 was detected, which was also dependent on RNA (Fig. 5c). These data suggested that Lar7, LSm2–8 and Trt1 independently bind to TER1 to form the telomerase ribonucleoprotein complex.
Summary: nucleolus is retained as an ancillary annotation.
Reason: Curated phylogenetic evidence supports an ancillary nucleolar RNA-processing role, consistent with Lsm2-7 association with snoRNA in budding yeast. This is compatible with conserved RNA-binding ring biology but is less directly established for fission yeast Lsm6 than its Lsm1-7 and Lsm2-8 roles.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
Summary: nucleolus is retained as an ancillary annotation.
Reason: Curated phylogenetic evidence supports an ancillary nucleolar RNA-processing role, consistent with Lsm2-7 association with snoRNA in budding yeast. This is compatible with conserved RNA-binding ring biology but is less directly established for fission yeast Lsm6 than its Lsm1-7 and Lsm2-8 roles.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
Summary: sno(s)RNA-containing ribonucleoprotein complex is retained as an ancillary annotation.
Reason: Curated phylogenetic evidence supports an ancillary nucleolar RNA-processing role, consistent with Lsm2-7 association with snoRNA in budding yeast. This is compatible with conserved RNA-binding ring biology but is less directly established for fission yeast Lsm6 than its Lsm1-7 and Lsm2-8 roles.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
Reason: Lsm6 is shared by the cytoplasmic Lsm1-7 ring, whose conserved association with Pat1 and decapping machinery underlies mRNA turnover and P-body residence. Target-specific ring reconstitution supports the complex assignment; P-body residence remains a conserved localization inference.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
The multi-ORF expression system was assembled into a single plasmid through ligation independent cloning as described for Lsm2–8, with the ORFs assembled in order Lsm6, Lsm3, Lsm2, Lsm1, Lsm4, Lsm7, and Lsm5.
Reason: Lsm6 is shared by the cytoplasmic Lsm1-7 ring, whose conserved association with Pat1 and decapping machinery underlies mRNA turnover and P-body residence. Target-specific ring reconstitution supports the complex assignment; P-body residence remains a conserved localization inference.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
The multi-ORF expression system was assembled into a single plasmid through ligation independent cloning as described for Lsm2–8, with the ORFs assembled in order Lsm6, Lsm3, Lsm2, Lsm1, Lsm4, Lsm7, and Lsm5.
IDA PMID:22615807 Crystal structures of Lsm3, Lsm4 and Lsm5/6/7 from Schizosac...
ACCEPT
Summary: poly(U) RNA binding is supported.
Reason: Fission yeast Lsm5/6/7 subcomplex binds oligo(U) in RNA-binding assays, and intact Lsm rings reveal the RNA-recognition mechanism. This supports the subunit contribution to RNA binding without treating an isolated monomer as the physiological RNA-binding species.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
The multi-ORF expression system was assembled into a single plasmid through ligation independent cloning as described for Lsm2–8, with the ORFs assembled in order Lsm6, Lsm3, Lsm2, Lsm1, Lsm4, Lsm7, and Lsm5.
Summary: maturation of SSU-rRNA is retained as an ancillary annotation.
Reason: Curated phylogenetic evidence supports an ancillary nucleolar RNA-processing role, consistent with Lsm2-7 association with snoRNA in budding yeast. This is compatible with conserved RNA-binding ring biology but is less directly established for fission yeast Lsm6 than its Lsm1-7 and Lsm2-8 roles.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
IDA PMID:26292707 Structure of a yeast spliceosome at 3.6-angstrom resolution.
UNDECIDED
Summary: U2 snRNA binding is not fully resolved.
Reason: The accessible main text of PMID:26292707 describes Sm rings associated with U2 and U5, while fission yeast Lsm6 is experimentally established in Lsm RNA-binding rings. The exact protein identities and contacts underlying the PomBase U2/U5 assignment require resolution against the supplementary models and chain mappings. The broader spliceosome context is compatible with Lsm6 function, but it does not by itself settle this precise RNA or particle assignment.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
Summary: U4/U6 x U5 tri-snRNP complex is supported.
Reason: Lsm6 is a conserved subunit of the Lsm2-8 ring that binds U6 RNA and supports spliceosomal snRNP assembly and mRNA splicing. Fission yeast reconstitution and structures establish the target subunit within this RNA-recognition assembly.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
The multi-ORF expression system was assembled into a single plasmid through ligation independent cloning as described for Lsm2–8, with the ORFs assembled in order Lsm6, Lsm3, Lsm2, Lsm1, Lsm4, Lsm7, and Lsm5.
Summary: Sm-like protein family complex is supported.
Reason: Target-specific crystallography and reconstitution directly establish Lsm6 in Sm-fold ring complexes. The broad family-complex assertion is biologically supported independently of ARBA, although the named Lsm complexes are more informative.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
The multi-ORF expression system was assembled into a single plasmid through ligation independent cloning as described for Lsm2–8, with the ORFs assembled in order Lsm6, Lsm3, Lsm2, Lsm1, Lsm4, Lsm7, and Lsm5.
EXP PMID:22001694 Structure of the LSm657 complex: an assembly intermediate of...
ACCEPT
Summary: Lsm2-8 complex is supported.
Reason: Lsm6 is a conserved subunit of the Lsm2-8 ring that binds U6 RNA and supports spliceosomal snRNP assembly and mRNA splicing. Fission yeast reconstitution and structures establish the target subunit within this RNA-recognition assembly. The original PMID:22001694 annotation is retained at its stated evidential scope; accessible source text and the independent evidence cited here are considered together.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
The multi-ORF expression system was assembled into a single plasmid through ligation independent cloning as described for Lsm2–8, with the ORFs assembled in order Lsm6, Lsm3, Lsm2, Lsm1, Lsm4, Lsm7, and Lsm5.
EXP PMID:32518066 Molecular basis for the distinct cellular functions of the L...
ACCEPT
Summary: Lsm2-8 complex is supported.
Reason: Lsm6 is a conserved subunit of the Lsm2-8 ring that binds U6 RNA and supports spliceosomal snRNP assembly and mRNA splicing. Fission yeast reconstitution and structures establish the target subunit within this RNA-recognition assembly.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
The multi-ORF expression system was assembled into a single plasmid through ligation independent cloning as described for Lsm2–8, with the ORFs assembled in order Lsm6, Lsm3, Lsm2, Lsm1, Lsm4, Lsm7, and Lsm5.
IPI PMID:32518066 Molecular basis for the distinct cellular functions of the L...
ACCEPT
Summary: Lsm2-8 complex is supported.
Reason: Lsm6 is a conserved subunit of the Lsm2-8 ring that binds U6 RNA and supports spliceosomal snRNP assembly and mRNA splicing. Fission yeast reconstitution and structures establish the target subunit within this RNA-recognition assembly.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
The multi-ORF expression system was assembled into a single plasmid through ligation independent cloning as described for Lsm2–8, with the ORFs assembled in order Lsm6, Lsm3, Lsm2, Lsm1, Lsm4, Lsm7, and Lsm5.
NAS PMID:32518066 Molecular basis for the distinct cellular functions of the L...
ACCEPT
Summary: telomerase holoenzyme complex assembly is supported.
Reason: The nuclear Lsm2-8 ring protects telomerase RNA and supports telomerase assembly in fission yeast. This is a complex-level RNA-stabilization role, not reverse-transcriptase catalysis. The target is an experimentally established shared Lsm2-8 subunit.
The multi-ORF expression system was assembled into a single plasmid through ligation independent cloning as described for Lsm2–8, with the ORFs assembled in order Lsm6, Lsm3, Lsm2, Lsm1, Lsm4, Lsm7, and Lsm5.
Co-immunoprecipitation assays confirmed an interaction between Lsm3 and Lar7 (Fig. 5b), indicating that they co-exist as a complex. Their association was sensitive to the presence of RNase and was abolished in lar7-W103A and lar7-FV197EE mutants. In addition, an interaction between wild-type Lar7 and Trt1 was detected, which was also dependent on RNA (Fig. 5c). These data suggested that Lar7, LSm2–8 and Trt1 independently bind to TER1 to form the telomerase ribonucleoprotein complex.
TAS PMID:29422501 LARP7 family proteins have conserved function in telomerase ...
ACCEPT
Summary: telomerase holoenzyme complex assembly is supported.
Reason: The nuclear Lsm2-8 ring protects telomerase RNA and supports telomerase assembly in fission yeast. This is a complex-level RNA-stabilization role, not reverse-transcriptase catalysis. The target is an experimentally established shared Lsm2-8 subunit. The original PMID:29422501 annotation is retained at its stated evidential scope; accessible source text and the independent evidence cited here are considered together.
The multi-ORF expression system was assembled into a single plasmid through ligation independent cloning as described for Lsm2–8, with the ORFs assembled in order Lsm6, Lsm3, Lsm2, Lsm1, Lsm4, Lsm7, and Lsm5.
Co-immunoprecipitation assays confirmed an interaction between Lsm3 and Lar7 (Fig. 5b), indicating that they co-exist as a complex. Their association was sensitive to the presence of RNase and was abolished in lar7-W103A and lar7-FV197EE mutants. In addition, an interaction between wild-type Lar7 and Trt1 was detected, which was also dependent on RNA (Fig. 5c). These data suggested that Lar7, LSm2–8 and Trt1 independently bind to TER1 to form the telomerase ribonucleoprotein complex.
EXP PMID:22001694 Structure of the LSm657 complex: an assembly intermediate of...
ACCEPT
Summary: Lsm1-7-Pat1 complex is supported.
Reason: Lsm6 is shared by the cytoplasmic Lsm1-7 ring, whose conserved association with Pat1 and decapping machinery underlies mRNA turnover and P-body residence. Target-specific ring reconstitution supports the complex assignment; P-body residence remains a conserved localization inference. The original PMID:22001694 annotation is retained at its stated evidential scope; accessible source text and the independent evidence cited here are considered together.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
The multi-ORF expression system was assembled into a single plasmid through ligation independent cloning as described for Lsm2–8, with the ORFs assembled in order Lsm6, Lsm3, Lsm2, Lsm1, Lsm4, Lsm7, and Lsm5.
EXP PMID:32518066 Molecular basis for the distinct cellular functions of the L...
ACCEPT
Summary: Lsm1-7-Pat1 complex is supported.
Reason: Lsm6 is shared by the cytoplasmic Lsm1-7 ring, whose conserved association with Pat1 and decapping machinery underlies mRNA turnover and P-body residence. Target-specific ring reconstitution supports the complex assignment; P-body residence remains a conserved localization inference.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
The multi-ORF expression system was assembled into a single plasmid through ligation independent cloning as described for Lsm2–8, with the ORFs assembled in order Lsm6, Lsm3, Lsm2, Lsm1, Lsm4, Lsm7, and Lsm5.
Core Functions
RNA-binding component of nuclear Lsm2-8 supporting U6-dependent splicing and telomerase RNA assembly.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
The multi-ORF expression system was assembled into a single plasmid through ligation independent cloning as described for Lsm2–8, with the ORFs assembled in order Lsm6, Lsm3, Lsm2, Lsm1, Lsm4, Lsm7, and Lsm5.
Co-immunoprecipitation assays confirmed an interaction between Lsm3 and Lar7 (Fig. 5b), indicating that they co-exist as a complex. Their association was sensitive to the presence of RNase and was abolished in lar7-W103A and lar7-FV197EE mutants. In addition, an interaction between wild-type Lar7 and Trt1 was detected, which was also dependent on RNA (Fig. 5c). These data suggested that Lar7, LSm2–8 and Trt1 independently bind to TER1 to form the telomerase ribonucleoprotein complex.
Shared RNA-binding subunit of the cytoplasmic Lsm1-7-Pat1 mRNA-decay complex.
RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.
The multi-ORF expression system was assembled into a single plasmid through ligation independent cloning as described for Lsm2–8, with the ORFs assembled in order Lsm6, Lsm3, Lsm2, Lsm1, Lsm4, Lsm7, and Lsm5.
These computational predictions are reviewed separately from the GOA annotation set used for this review. The assessments below are from this project and do not constitute official GO annotations or endorsement by GO/UniProt. They are not included in the existing annotation review above.
Lsm6 participates in experimentally established Lsm RNA-binding rings. The broad Sm-like family-complex prediction is supported but less precise than the named Lsm2-8 and Lsm1-7-Pat1 complexes.
Review rationale: Fission yeast crystallography and biochemical reconstitution establish Lsm6 within Sm-fold RNA-binding rings. These primary results validate the broad Sm-like family-complex assertion independently of its ARBA overlap. GOA already contains the more specific Lsm2-8 and Lsm1-7-Pat1 complex annotations. The prediction is therefore correct but less informative than the established complex assignments.
Supporting Evidence:
PMID:22615807: "RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7."
PMID:32518066: "The multi-ORF expression system was assembled into a single plasmid through ligation independent cloning as described for Lsm2–8, with the ORFs assembled in order Lsm6, Lsm3, Lsm2, Lsm1, Lsm4, Lsm7, and Lsm5."