A negative elongation factor for human RNA polymerase II inhibits the anti-arrest transcript-cleavage factor TFIIS

Murali Palangat; Dan B Renner; David H Price; Robert Landick

doi:10.1073/pnas.0409405102

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A negative elongation factor for human RNA polymerase II inhibits the anti-arrest transcript-cleavage factor TFIIS

Journal article

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A negative elongation factor for human RNA polymerase II inhibits the anti-arrest transcript-cleavage factor TFIIS

Murali Palangat, Dan B Renner, David H Price and Robert Landick

Proceedings of the National Academy of Sciences - PNAS, Vol.102(42), pp.15036-15041

10/18/2005

DOI: 10.1073/pnas.0409405102

PMCID: PMC1257689

PMID: 16214896

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Abstract

Formation of productive transcription complexes after promoter escape by RNA polymerase II is a major event in eukaryotic gene regulation. Both negative and positive factors control this step. The principal negative elongation factor (NELF) contains four polypeptides and requires for activity the two-polypeptide 5,6-dichloro-1-β- d -ribobenzimidazole-sensitivity inducing factor (DSIF). DSIF/NELF inhibits early transcript elongation until it is counteracted by the positive elongation factor P-TEFb. We report a previously undescribed activity of DSIF/NELF, namely inhibition of the transcript cleavage factor TFIIS. These two activities of DSIF/NELF appear to be mechanistically distinct. Inhibition of nucleotide addition requires ≥18 nt of nascent RNA, whereas inhibition of TFIIS occurs at all transcript lengths. Because TFIIS promotes escape from promoter-proximal pauses by stimulating cleavage of back-tracked nascent RNA, TFIIS inhibition may help DSIF/NELF negatively regulate productive transcription.

transcription elongation

Biological Sciences

backtracking

pausing

Details

Title: Subtitle: A negative elongation factor for human RNA polymerase II inhibits the anti-arrest transcript-cleavage factor TFIIS
Creators: Murali Palangat - Department of Bacteriology, University of Wisconsin, Madison, WI 53706; and
Dan B Renner - Department of Bacteriology, University of Wisconsin, Madison, WI 53706; and
David H Price - Department of Bacteriology, University of Wisconsin, Madison, WI 53706; and
Robert Landick - Department of Bacteriology, University of Wisconsin, Madison, WI 53706; and
Resource Type: Journal article
Publication Details: Proceedings of the National Academy of Sciences - PNAS, Vol.102(42), pp.15036-15041
DOI: 10.1073/pnas.0409405102
PMID: 16214896
PMCID: PMC1257689
NLM abbreviation: Proc Natl Acad Sci U S A
ISSN: 0027-8424
eISSN: 1091-6490
Publisher: National Academy of Sciences
Language: English
Date published: 10/18/2005
Academic Unit: Biochemistry and Molecular Biology
Record Identifier: 9984024560202771

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