Literature DB >> 7649479

HMG17 is a chromatin-specific transcriptional coactivator that increases the efficiency of transcription initiation.

S M Paranjape1, A Krumm, J T Kadonaga.   

Abstract

We have examined the effect of HMG17 on transcription by RNA polymerase II by the assembly and analysis of HMG17-containing chromatin templates consisting of regularly spaced nucleosomal arrays. Structural analysis of the chromatin indicated that HMG17 is incorporated into chromatin in a physiological manner with the full complement of core histones. The transcriptional studies revealed that HMG17 stimulates transcription in conjunction with the sequence-specific activator GAL4-VP16. This effect was observed with chromatin, but not with non-nucleosomal templates, and required the presence of HMG17 during chromatin assembly. The incorporation of HMG17 into chromatin resulted in a 7- to 40-fold stimulation of GAL4-VP16-activated transcription to levels that were comparable to those observed with histone-free DNA templates. In contrast, transcription from HMG17-containing chromatin was not detectable in the absence of GAL4-VP16 or with a GAL4 derivative [GAL4(1-147)] lacking the VP16 activation domain. Finally, the incorporation of HMG17 into chromatin was found to increase the efficiency of transcription initiation, but not the extent of transcriptional elongation. Thus, HMG17 is a chromatin-specific transcriptional coactivator that increases the efficiency of initiation of transcription by RNA polymerase II.

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Year:  1995        PMID: 7649479     DOI: 10.1101/gad.9.16.1978

Source DB:  PubMed          Journal:  Genes Dev        ISSN: 0890-9369            Impact factor:   11.361


  29 in total

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2.  Retinoid-induced chromatin structure alterations in the retinoic acid receptor beta2 promoter.

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3.  Alleviation of histone H1-mediated transcriptional repression and chromatin compaction by the acidic activation region in chromosomal protein HMG-14.

Authors:  H F Ding; M Bustin; U Hansen
Journal:  Mol Cell Biol       Date:  1997-10       Impact factor: 4.272

4.  Nucleosome binding by the polymerase I transactivator upstream binding factor displaces linker histone H1.

Authors:  M Kermekchiev; J L Workman; C S Pikaard
Journal:  Mol Cell Biol       Date:  1997-10       Impact factor: 4.272

5.  Activation domain-specific and general transcription stimulation by native histone acetyltransferase complexes.

Authors:  K Ikeda; D J Steger; A Eberharter; J L Workman
Journal:  Mol Cell Biol       Date:  1999-01       Impact factor: 4.272

Review 6.  Considerations of transcriptional control mechanisms: do TFIID-core promoter complexes recapitulate nucleosome-like functions?

Authors:  A Hoffmann; T Oelgeschläger; R G Roeder
Journal:  Proc Natl Acad Sci U S A       Date:  1997-08-19       Impact factor: 11.205

7.  Chromosomal proteins HMGN3a and HMGN3b regulate the expression of glycine transporter 1.

Authors:  Katherine L West; Meryl A Castellini; Melinda K Duncan; Michael Bustin
Journal:  Mol Cell Biol       Date:  2004-05       Impact factor: 4.272

8.  Increased tumorigenicity and sensitivity to ionizing radiation upon loss of chromosomal protein HMGN1.

Authors:  Yehudit Birger; Frédéric Catez; Takashi Furusawa; Jae-Hwan Lim; Marta Prymakowska-Bosak; Katherine L West; Yuri V Postnikov; Diana C Haines; Michael Bustin
Journal:  Cancer Res       Date:  2005-08-01       Impact factor: 12.701

9.  cAMP-response element-binding protein (CREB) controls MSK1-mediated phosphorylation of histone H3 at the c-fos promoter in vitro.

Authors:  Miho Shimada; Tomoyoshi Nakadai; Aya Fukuda; Koji Hisatake
Journal:  J Biol Chem       Date:  2010-01-20       Impact factor: 5.157

Review 10.  Regulation of chromatin structure and function by HMGN proteins.

Authors:  Yuri Postnikov; Michael Bustin
Journal:  Biochim Biophys Acta       Date:  2009-11-27
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