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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1999-4-27
pubmed:abstractText
DRB is a classic inhibitor of transcription elongation by RNA polymerase II (pol II). Since DRB generally affects class II genes, factors involved in this process must play fundamental roles in pol II elongation. Recently, two elongation factors essential for DRB action were identified, namely DSIF and P-TEFb. Here we describe the identification and purification from HeLa nuclear extract of a third protein factor required for DRB-sensitive transcription. This factor, termed negative elongation factor (NELF), cooperates with DSIF and strongly represses pol II elongation. This repression is reversed by P-TEFb-dependent phosphorylation of the pol II C-terminal domain. NELF is composed of five polypeptides, the smallest of which is identical to RD, a putative RNA-binding protein of unknown function. This study reveals a molecular mechanism for DRB action and a regulatory network of positive and negative elongation factors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/DSIF protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Dichlororibofuranosylbenzimidazole, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Positive Transcriptional..., http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/RDBP protein, human, http://linkedlifedata.com/resource/pubmed/chemical/RNA Polymerase II, http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/SUPT4H1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/Transcriptional Elongation Factors
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
97
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
41-51
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:10199401-Amino Acid Sequence, pubmed-meshheading:10199401-Cloning, Molecular, pubmed-meshheading:10199401-Dichlororibofuranosylbenzimidazole, pubmed-meshheading:10199401-Dimerization, pubmed-meshheading:10199401-HeLa Cells, pubmed-meshheading:10199401-Humans, pubmed-meshheading:10199401-Kinetics, pubmed-meshheading:10199401-Molecular Sequence Data, pubmed-meshheading:10199401-Nuclear Proteins, pubmed-meshheading:10199401-Positive Transcriptional Elongation Factor B, pubmed-meshheading:10199401-Protein-Serine-Threonine Kinases, pubmed-meshheading:10199401-RNA Polymerase II, pubmed-meshheading:10199401-RNA-Binding Proteins, pubmed-meshheading:10199401-Repressor Proteins, pubmed-meshheading:10199401-Transcription Factors, pubmed-meshheading:10199401-Transcriptional Elongation Factors, pubmed-meshheading:10199401-Tumor Cells, Cultured
pubmed:year
1999
pubmed:articleTitle
NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation.
pubmed:affiliation
Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't