Literature DB >> 11163204

Coordinate regulation of yeast ribosomal protein genes is associated with targeted recruitment of Esa1 histone acetylase.

J L Reid1, V R Iyer, P O Brown, K Struhl.   

Abstract

The Esa1-containing NuA4 histone acetylase complex can interact with activation domains in vitro and stimulate transcription on reconstituted chromatin templates. In yeast cells, Esa1 is targeted to a small subset of promoters in an activator-specific manner. Esa1 is specifically recruited to ribosomal protein (RP) promoters, and this recruitment appears to require binding by Rap1 or Abf1. Esa1 is important for RP transcription, and Esa1 recruitment to RP promoters correlates with coordinate regulation of RP genes in response to growth stimuli. However, following Esa1 depletion, H4 acetylation decreases dramatically at many loci, but transcription is not generally affected. Therefore, the transcription-associated targeted recruitment of Esa1 to RP promoters occurs in a background of more global nontargeted acetylation that is itself not required for transcription.

Entities:  

Mesh:

Substances:

Year:  2000        PMID: 11163204     DOI: 10.1016/s1097-2765(00)00128-3

Source DB:  PubMed          Journal:  Mol Cell        ISSN: 1097-2765            Impact factor:   17.970


  149 in total

1.  Histone acetylation at promoters is differentially affected by specific activators and repressors.

Authors:  J Deckert; K Struhl
Journal:  Mol Cell Biol       Date:  2001-04       Impact factor: 4.272

2.  Dynamics of global histone acetylation and deacetylation in vivo: rapid restoration of normal histone acetylation status upon removal of activators and repressors.

Authors:  Yael Katan-Khaykovich; Kevin Struhl
Journal:  Genes Dev       Date:  2002-03-15       Impact factor: 11.361

3.  Genome-wide location and regulated recruitment of the RSC nucleosome-remodeling complex.

Authors:  Huck Hui Ng; François Robert; Richard A Young; Kevin Struhl
Journal:  Genes Dev       Date:  2002-04-01       Impact factor: 11.361

4.  Rap1p and other transcriptional regulators can function in defining distinct domains of gene expression.

Authors:  Qun Yu; Runxiang Qiu; Travis B Foland; Dan Griesen; Carl S Galloway; Ya-Hui Chiu; Joseph Sandmeier; James R Broach; Xin Bi
Journal:  Nucleic Acids Res       Date:  2003-02-15       Impact factor: 16.971

5.  SWI/SNF-dependent long-range remodeling of yeast HIS3 chromatin.

Authors:  Yeonjung Kim; David J Clark
Journal:  Proc Natl Acad Sci U S A       Date:  2002-11-13       Impact factor: 11.205

6.  Global control of histone modification by the anaphase-promoting complex.

Authors:  Vijay Ramaswamy; Jessica S Williams; Karen M Robinson; Richelle L Sopko; Michael C Schultz
Journal:  Mol Cell Biol       Date:  2003-12       Impact factor: 4.272

7.  Targeted histone acetylation at the yeast CUP1 promoter requires the transcriptional activator, the TATA boxes, and the putative histone acetylase encoded by SPT10.

Authors:  Chang-Hui Shen; Benoit P Leblanc; Carolyn Neal; Ramin Akhavan; David J Clark
Journal:  Mol Cell Biol       Date:  2002-09       Impact factor: 4.272

Review 8.  The different (sur)faces of Rap1p.

Authors:  B Piña; J Fernández-Larrea; N García-Reyero; F-Z Idrissi
Journal:  Mol Genet Genomics       Date:  2003-01-25       Impact factor: 3.291

9.  The Yaf9 component of the SWR1 and NuA4 complexes is required for proper gene expression, histone H4 acetylation, and Htz1 replacement near telomeres.

Authors:  Haiying Zhang; Daniel O Richardson; Douglas N Roberts; Rhea Utley; Hediye Erdjument-Bromage; Paul Tempst; Jacques Côté; Bradley R Cairns
Journal:  Mol Cell Biol       Date:  2004-11       Impact factor: 4.272

10.  Essential function of p300 acetyltransferase activity in heart, lung and small intestine formation.

Authors:  Noriko Shikama; Werner Lutz; Ralph Kretzschmar; Nadine Sauter; Jeanne-Françoise Roth; Silvia Marino; Jonas Wittwer; Alexander Scheidweiler; Richard Eckner
Journal:  EMBO J       Date:  2003-10-01       Impact factor: 11.598

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.