Revealing the functions of TFIIB

The TFIIB linker domain stimulates the catalytic activity of archaeal RNAP. By characterising a range of super-stimulating mutants we identified a novel rate-limiting step in transcription initiation. Our results help to interpret structural findings and pave the way towards higher-resolution struct...

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Bibliographic Details
Published inTranscription Vol. 2; no. 6; pp. 254 - 257
Main Authors Weinzierl, Robert O.J., Wiesler, Simone C.
Format Journal Article
LanguageEnglish
Published United States Taylor & Francis 01.11.2011
Landes Bioscience
Subjects
Amino Acid Sequence
Archaeal Proteins - chemistry
Archaeal Proteins - genetics
Archaeal Proteins - metabolism
Binding
Biology
Bioscience
Calcium
Cancer
Cell
Crystallography, X-Ray
Cycle
DNA-Directed RNA Polymerases - chemistry
DNA-Directed RNA Polymerases - genetics
DNA-Directed RNA Polymerases - metabolism
Landes
Methanococcales - genetics
Methanococcales - metabolism
Models, Molecular
Mutation
Organogenesis
Point of View
Protein Binding
Protein Structure, Tertiary
Proteins
Sequence Homology, Amino Acid
Transcription Factor TFIIB - chemistry
Transcription Factor TFIIB - genetics
Transcription Factor TFIIB - metabolism
Transcription, Genetic
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Summary:The TFIIB linker domain stimulates the catalytic activity of archaeal RNAP. By characterising a range of super-stimulating mutants we identified a novel rate-limiting step in transcription initiation. Our results help to interpret structural findings and pave the way towards higher-resolution structures of the RNAP-TFIIB linker interface.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:2154-1264
2154-1272
DOI:10.4161/trns.2.6.18076