Literature DB >> 11487468

You bet-cha: a novel family of transcriptional regulators.

B Florence1, D V Faller.   

Abstract

The BET proteins are a novel class of transcriptional regulators whose members can be found in animals, plants and fungi. Founding members are Human RING3, Drosophila Fsh and yeast Bdf1p. BET proteins are distinguished by an N-terminal bromodomain or bromodomains and an ET domain. As predicted by the presence of the bromodomain(s), these proteins have been found to be associated with chromatin. The poorly characterized ET domain functions as a protein-protein interaction motif and may be part of a serine-kinase activity. Other regions ("modular domains"), which are conserved only in certain BET proteins, are likely to provide sub-family specific functions. Genetic, biochemical and molecular techniques have implicated BET proteins in functions as diverse as meiosis, cell cycle control and homeosis. The data suggest that BET proteins may modulate chromatin structure and affect transcription via a sequence-independent mechanism. This review will attempt to summarize current research on BET proteins and envision where future research is likely to lead.

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Year:  2001        PMID: 11487468     DOI: 10.2741/florence

Source DB:  PubMed          Journal:  Front Biosci        ISSN: 1093-4715


  88 in total

1.  Oncogenesis by sequestration of CBP/p300 in transcriptionally inactive hyperacetylated chromatin domains.

Authors:  Nicolas Reynoird; Brian E Schwartz; Manuela Delvecchio; Karin Sadoul; David Meyers; Chandrani Mukherjee; Cécile Caron; Hiroshi Kimura; Sophie Rousseaux; Philip A Cole; Daniel Panne; Christopher A French; Saadi Khochbin
Journal:  EMBO J       Date:  2010-07-30       Impact factor: 11.598

Review 2.  Transcription and post-transcriptional regulation of spermatogenesis.

Authors:  Anilkumar Bettegowda; Miles F Wilkinson
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2010-05-27       Impact factor: 6.237

Review 3.  BET domain co-regulators in obesity, inflammation and cancer.

Authors:  Anna C Belkina; Gerald V Denis
Journal:  Nat Rev Cancer       Date:  2012-06-22       Impact factor: 60.716

4.  Interaction of bovine papillomavirus E2 protein with Brd4 stabilizes its association with chromatin.

Authors:  Maria G McPhillips; Keiko Ozato; Alison A McBride
Journal:  J Virol       Date:  2005-07       Impact factor: 5.103

5.  Brd4 is required for e2-mediated transcriptional activation but not genome partitioning of all papillomaviruses.

Authors:  M G McPhillips; J G Oliveira; J E Spindler; R Mitra; A A McBride
Journal:  J Virol       Date:  2006-10       Impact factor: 5.103

6.  Identification of transcription complexes that contain the double bromodomain protein Brd2 and chromatin remodeling machines.

Authors:  Gerald V Denis; Mark E McComb; Douglas V Faller; Anupama Sinha; Paul B Romesser; Catherine E Costello
Journal:  J Proteome Res       Date:  2006-03       Impact factor: 4.466

7.  Brd4-independent transcriptional repression function of the papillomavirus e2 proteins.

Authors:  Michal-Ruth Schweiger; Matthias Ottinger; Jianxin You; Peter M Howley
Journal:  J Virol       Date:  2007-07-11       Impact factor: 5.103

Review 8.  Replication and partitioning of papillomavirus genomes.

Authors:  Alison A McBride
Journal:  Adv Virus Res       Date:  2008       Impact factor: 9.937

9.  Bromo- and extraterminal domain chromatin regulators serve as cofactors for murine leukemia virus integration.

Authors:  Saumya Shree Gupta; Tobias Maetzig; Goedele N Maertens; Azar Sharif; Michael Rothe; Magdalena Weidner-Glunde; Melanie Galla; Axel Schambach; Peter Cherepanov; Thomas F Schulz
Journal:  J Virol       Date:  2013-09-18       Impact factor: 5.103

10.  Solution structure of the extraterminal domain of the bromodomain-containing protein BRD4.

Authors:  Yi-Jan Lin; Takashi Umehara; Makoto Inoue; Kohei Saito; Takanori Kigawa; Moon-Kyoo Jang; Keiko Ozato; Shigeyuki Yokoyama; Balasundaram Padmanabhan; Peter Güntert
Journal:  Protein Sci       Date:  2008-09-24       Impact factor: 6.725

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