Reference: Sterner DE, et al. (2002) The SANT domain of Ada2 is required for normal acetylation of histones by the yeast SAGA complex. J Biol Chem 277(10):8178-86

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Abstract


Transcription is regulated through chromatin remodeling and histone modification, mediated by large protein complexes. Histone and nucleosome interaction has been shown to be mediated by specific chromatin domains called bromodomains and chromodomains. Here we provide evidence for a similar function of two additional domains within the yeast SAGA complex, containing the histone acetyltransferase Gcn5. We have analyzed deletion and substitution mutations within Gcn5 and Ada2, an interacting protein within SAGA, and have identified substrate recognition functions within the SANT domain of Ada2 and regions of the histone acetyltransferase domain of Gcn5 that are distinct from catalytic function itself. These results suggest that histone and nucleosomal substrate recognition by SAGA involves multiple conserved domains and proteins, beyond those that have been previously identified.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't | Research Support, U.S. Gov't, Non-P.H.S. | Research Support, U.S. Gov't, P.H.S.
Authors
Sterner DE, Wang X, Bloom MH, Simon GM, Berger SL
Primary Lit For
GCN5 | ADA2 | SAGA complex

Interaction Annotations


Genetic Interactions

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Interactor Interactor Allele Assay Annotation Action Phenotype SGA score P-value Source Reference

Physical Interactions 4 entries for 5 genes

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InteractorInteractorAssayAnnotationActionModification
ADA2TAF6Co-purificationmanually curatedHit-BaitNo Modification
NGG1TAF6Co-purificationmanually curatedHit-BaitNo Modification
TAF12TAF6Co-purificationmanually curatedHit-BaitNo Modification
TAF6SPT20Co-purificationmanually curatedBait-HitNo Modification
Showing 1 to 4 of 4 entries