Crystal structure of GCN5 PCAF N-terminal domain reveals atypical ubiquitin ligase structure-Reference-Cited by-同舟云学术

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Crystal structure of GCN5 PCAF N-terminal domain reveals atypical ubiquitin ligase structure

Published:2020-10 Issue:43 Volume:295 Page:14630-14639
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Toma-Fukai Sachiko,Hibi Ryota,Naganuma Takao,Sakai Mashito,Saijo Shinya,Shimizu Nobutaka,Matsumoto Michihiro,Shimizu Toshiyuki

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference38 articles.

1. Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation;Brownell;Cell.,1996

2. Acetylation of histones and transcription-related factors;Sterner;Microbiol. Mol. Biol. Rev.,2000

3. Structure of SAGA and mechanism of TBP deposition on gene promoters;Papai;Nature,2020

4. Structure of the transcription coactivator SAGA;Wang;Nature,2020

5. Expanded lysine acetylation specificity of Gcn5 in native complexes;Grant;J. Biol. Chem.,1999

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