Transcription initiation constitutes a major checkpoint in gene regulation across all living organisms. Control of chromatin function is tightly linked to this checkpoint, which is best illustrated by the SAGA coactivator. This evolutionary conserved complex of 18-20 subunits was first discovered as a Gcn5p-containing histone acetyltransferase, but it also integrates a histone H2B deubiquitinase. The SAGA subunits are organized in a modular fashion around its central core. Strikingly, this central module of SAGA shares a number of proteins with the central core of the basal transcription factor TFIID. In this review I will compare the SAGA and TFIID complexes with respect to their shared subunits, structural organization, enzymatic activities and chromatin binding. I will place a special emphasis on the ancestry of SAGA and TFIID subunits, which suggests that these complexes evolved to control the activity of TBP (TATA-binding protein) in directing the assembly of transcription initiation complexes.

• PMID: 32673655
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Reference Type

Journal Article | Research Support, Non-U.S. Gov't | Review

Authors

Timmers HTM

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SPT7 | SGF73 | SPT3 | DBF4 | SUS1 | RVB1 | TAF6 | UBP8 | TIR1 | TEL2 | CHD1 | ... Show allTAF12 | SGF29 | TTI2 | TRA1 | TAF10 | NGG1 | GCN5 | PRP5 | YRA1 | CDC7 | RVB2 | HFI1 | ADA2 | CSE4 | TAF5 | SNF1 | UBP10 | TAF9 | TIR2 | ASA1 | SPT20 | SGF11 | SPT8 | MEX67 | TTI1 | SAGA complex | General transcription factor complex TFIID Show fewer