Literature DB >> 10916156

Control of elongation by RNA polymerase II.

J W Conaway1, A Shilatifard, A Dvir, R C Conaway.   

Abstract

The elongation stage of eukaryotic mRNA synthesis can be regulated by transcription factors that interact directly with the RNA polymerase II (pol II) elongation complex and by activities that modulate the structure of its chromatin template. Recent studies have revealed new elongation factors and have implicated the general initiation factors TFIIE, TFIIF and TFIIH, as well as the C-terminal domain (CTD) of the largest subunit of pol II, in elongation. The recently reported high-resolution crystal structure of RNA polymerase II, which provides insight into the architecture of the elongation complex, marks a new era of investigation into transcription elongation.

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Year:  2000        PMID: 10916156     DOI: 10.1016/s0968-0004(00)01615-7

Source DB:  PubMed          Journal:  Trends Biochem Sci        ISSN: 0968-0004            Impact factor:   13.807


  71 in total

1.  ATP bound to the origin recognition complex is important for preRC formation.

Authors:  R D Klemm; S P Bell
Journal:  Proc Natl Acad Sci U S A       Date:  2001-07-17       Impact factor: 11.205

2.  Analysis of the open region of RNA polymerase II transcription complexes in the early phase of elongation.

Authors:  U Fiedler; H T Timmers
Journal:  Nucleic Acids Res       Date:  2001-07-01       Impact factor: 16.971

3.  Interaction between P-TEFb and the C-terminal domain of RNA polymerase II activates transcriptional elongation from sites upstream or downstream of target genes.

Authors:  Ran Taube; Xin Lin; Dan Irwin; Koh Fujinaga; B Matija Peterlin
Journal:  Mol Cell Biol       Date:  2002-01       Impact factor: 4.272

4.  RNA polymerase II complexes in the very early phase of transcription are not susceptible to TFIIS-induced exonucleolytic cleavage.

Authors:  Robert Sijbrandi; Ulrike Fiedler; H Th Marc Timmers
Journal:  Nucleic Acids Res       Date:  2002-06-01       Impact factor: 16.971

5.  Molecular mechanism of recruitment of TFIIF- associating RNA polymerase C-terminal domain phosphatase (FCP1) by transcription factor IIF.

Authors:  Katsuhiko Kamada; Robert G Roeder; Stephen K Burley
Journal:  Proc Natl Acad Sci U S A       Date:  2003-02-18       Impact factor: 11.205

6.  The C-terminal domain phosphatase and transcription elongation activities of FCP1 are regulated by phosphorylation.

Authors:  Erika M Friedl; William S Lane; Hediye Erdjument-Bromage; Paul Tempst; Danny Reinberg
Journal:  Proc Natl Acad Sci U S A       Date:  2003-02-18       Impact factor: 11.205

7.  In vivo evidence that defects in the transcriptional elongation factors RPB2, TFIIS, and SPT5 enhance upstream poly(A) site utilization.

Authors:  Yajun Cui; Clyde L Denis
Journal:  Mol Cell Biol       Date:  2003-11       Impact factor: 4.272

8.  The FCP1 phosphatase interacts with RNA polymerase II and with MEP50 a component of the methylosome complex involved in the assembly of snRNP.

Authors:  Paolo Licciardo; Stefano Amente; Luca Ruggiero; Maria Monti; Piero Pucci; Luigi Lania; Barbara Majello
Journal:  Nucleic Acids Res       Date:  2003-02-01       Impact factor: 16.971

9.  An RNA polymerase pause site is associated with the immunoglobulin mus poly(A) site.

Authors:  Martha L Peterson; Shannon Bertolino; Frankie Davis
Journal:  Mol Cell Biol       Date:  2002-08       Impact factor: 4.272

10.  RNA polymerase stalling at developmental control genes in the Drosophila melanogaster embryo.

Authors:  Julia Zeitlinger; Alexander Stark; Manolis Kellis; Joung-Woo Hong; Sergei Nechaev; Karen Adelman; Michael Levine; Richard A Young
Journal:  Nat Genet       Date:  2007-11-11       Impact factor: 38.330

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