laeA is a nuclear, SAM-dependent methyltransferase (velvet-complex subunit) that acts as a global regulator of secondary metabolism in Aspergillus nidulans and related Aspergilli. Deletion of laeA blocks expression of diverse secondary-metabolite gene clusters (sterigmatocystin, penicillin, lovastatin), while overexpression increases them; LaeA acts at the level of chromatin/cluster activation. Biochemically LaeA is a methyltransferase that undergoes automethylation generating S-methylmethionine; it forms the VelB-VeA-LaeA velvet complex, coupling development (including sexual sporulation) to secondary metabolism, and contributes to chemical defense/virulence via the metabolites it controls.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0008168 methyltransferase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Core molecular function. LaeA is a methyltransferase. Reason: SAM-dependent methyltransferase; concordant with IDA evidence (PMID:23532849). |
| GO:0005634 nucleus | IEA GO_REF:0000044 | ACCEPT | Summary: Nuclear localization (UniProt mapping). Reason: Consistent with experimentally determined nuclear localization. |
| GO:0008168 methyltransferase activity | IDA PMID:23532849 A novel automethylation reaction in the Aspergillus nidulans... | ACCEPT | Summary: Core molecular function (direct). Methyltransferase activity. Reason: Biochemical demonstration of a methyltransferase reaction: LaeA automethylates a methionine residue to generate S-methylmethionine. Note the scope limit — the same study failed to find any methyl-accepting substrate, so the demonstrated activity is automethylation rather than trans-methylation of a partner protein. Supporting Evidence: PMID:23532849 LaeA is the first protein to exhibit automethylation at a methionine residue. PMID:23532849 However, in each experiment LaeA was shown to self-methylate. |
| GO:0030437 ascospore formation | IMP PMID:20935144 Suppressor mutagenesis identifies a velvet complex remediato... | KEEP AS NON CORE | Summary: LaeA promotes ascospore (sexual) formation (developmental role). Reason: LaeA, via the velvet complex, promotes sexual development; a real but non-core role relative to its SM-regulation function. |
| GO:0030437 ascospore formation | IMP PMID:21152013 LaeA control of velvet family regulatory proteins for light-... | KEEP AS NON CORE | Summary: LaeA promotes ascospore formation (duplicate). Reason: Velvet-complex-dependent developmental role; non-core. Supporting Evidence: PMID:21152013 In the dark, VeA bridges VelB and LaeA to form the VelB-VeA-LaeA (velvet) complex |
| GO:0045460 sterigmatocystin metabolic process | IMP PMID:15075281 LaeA, a regulator of secondary metabolism in Aspergillus spp... | KEEP AS NON CORE | Summary: LaeA regulates sterigmatocystin metabolism (regulatory reach). Reason: LaeA controls the ST gene cluster; annotated here to the metabolic process via acts_upstream_of_or_within. The precise role is regulatory (see GO:0010914); kept as non-core to avoid duplicating the regulation term. Supporting Evidence: PMID:15075281 Deletion of laeA (DeltalaeA) blocks the expression of metabolic gene clusters, including the sterigmatocystin (carcinogen), penicillin (antibiotic), and lovastatin (antihypercholesterolemic agent) gene clusters |
| GO:0045460 sterigmatocystin metabolic process | IMP PMID:18556559 VelB/VeA/LaeA complex coordinates light signal with fungal d... | KEEP AS NON CORE | Summary: LaeA regulates ST metabolism (duplicate). Reason: Regulatory reach over the ST cluster; non-core relative to GO:0010914. |
| GO:0010914 positive regulation of sterigmatocystin biosynthetic process | IMP PMID:18556559 VelB/VeA/LaeA complex coordinates light signal with fungal d... | ACCEPT | Summary: Core process. LaeA positively regulates sterigmatocystin biosynthesis. Reason: Deletion of laeA blocks ST cluster expression; overexpression increases it. Supporting Evidence: PMID:15075281 Deletion of laeA (DeltalaeA) blocks the expression of metabolic gene clusters, including the sterigmatocystin (carcinogen), penicillin (antibiotic), and lovastatin (antihypercholesterolemic agent) gene clusters |
| GO:0042316 penicillin metabolic process | IMP PMID:15075281 LaeA, a regulator of secondary metabolism in Aspergillus spp... | KEEP AS NON CORE | Summary: LaeA regulates penicillin metabolism (regulatory reach). Reason: LaeA controls the penicillin cluster; the metabolic-process annotation reflects regulatory reach, captured precisely by GO:0033246. Supporting Evidence: PMID:15075281 Deletion of laeA (DeltalaeA) blocks the expression of metabolic gene clusters, including the sterigmatocystin (carcinogen), penicillin (antibiotic), and lovastatin (antihypercholesterolemic agent) gene clusters |
| GO:1900376 regulation of secondary metabolite biosynthetic process | IMP PMID:15075281 LaeA, a regulator of secondary metabolism in Aspergillus spp... | ACCEPT | Summary: Core process. LaeA is a global regulator of secondary-metabolite biosynthesis. Reason: LaeA regulates expression of multiple secondary-metabolite gene clusters; this is its central function. Supporting Evidence: PMID:15075281 We present here a novel Aspergillus nuclear protein, LaeA, as a global regulator of secondary metabolism in this genus |
| GO:0075296 positive regulation of ascospore formation | IMP PMID:21152013 LaeA control of velvet family regulatory proteins for light-... | KEEP AS NON CORE | Summary: LaeA positively regulates ascospore formation (developmental). Reason: Velvet-complex-dependent sexual-development role; non-core. |
| GO:0075296 positive regulation of ascospore formation | IMP PMID:20935144 Suppressor mutagenesis identifies a velvet complex remediato... | KEEP AS NON CORE | Summary: LaeA positively regulates ascospore formation (duplicate). Reason: Non-core developmental role. |
| GO:0051701 biological process involved in interaction with host | IMP PMID:17686752 Secondary chemicals protect mould from fungivory. | KEEP AS NON CORE | Summary: LaeA affects fungus-fungivore interaction via secondary metabolites (loose term fit). Reason: Loss of LaeA-controlled secondary metabolites reduces protection against fungivory; the term 'interaction with host' is a loose fit (the springtail is a predator, not a host), so kept as a non-core, indirect ecological role. |
| GO:0005634 nucleus | IDA PMID:18556559 VelB/VeA/LaeA complex coordinates light signal with fungal d... | ACCEPT | Summary: Nuclear localization (direct). Reason: Direct assay; consistent with LaeA nuclear function. |
| GO:0008168 methyltransferase activity | IMP PMID:16968230 Secondary metabolic gene cluster silencing in Aspergillus ni... | ACCEPT | Summary: Core molecular function (IMP). Methyltransferase activity. Reason: Point-mutation of the SAM-binding motif abolishes LaeA function, supporting a methyltransferase activity requirement. |
| GO:0005634 nucleus | IDA PMID:15075281 LaeA, a regulator of secondary metabolism in Aspergillus spp... | ACCEPT | Summary: Nuclear localization (direct). Reason: Direct assay from the founding LaeA characterization. |
| GO:0010914 positive regulation of sterigmatocystin biosynthetic process | IMP PMID:15075281 LaeA, a regulator of secondary metabolism in Aspergillus spp... | ACCEPT | Summary: Core process (duplicate). Positive regulation of sterigmatocystin biosynthesis. Reason: Consistent with LaeA's control of the ST cluster. Supporting Evidence: PMID:15075281 Deletion of laeA (DeltalaeA) blocks the expression of metabolic gene clusters, including the sterigmatocystin (carcinogen), penicillin (antibiotic), and lovastatin (antihypercholesterolemic agent) gene clusters |
| GO:0033246 positive regulation of penicillin metabolic process | IMP PMID:15075281 LaeA, a regulator of secondary metabolism in Aspergillus spp... | ACCEPT | Summary: Core process. LaeA positively regulates penicillin biosynthesis. Reason: LaeA is required for expression of the penicillin biosynthetic cluster. Supporting Evidence: PMID:15075281 Deletion of laeA (DeltalaeA) blocks the expression of metabolic gene clusters, including the sterigmatocystin (carcinogen), penicillin (antibiotic), and lovastatin (antihypercholesterolemic agent) gene clusters |
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