ArticleProtein science : a publication of the Protein Society2000
Structure of a (Cys3His) zinc ribbon, a ubiquitous motif in archaeal and eucaryal transcription.
Article in Protein science : a publication of the Protein Society, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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23 citing papers in PubMed, 69 citations in OpenAlex.
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- Host and Viral Zinc-Finger Proteins in COVID-19.International journal of molecular sciences · 2022Review
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- Evolutionary convergence and divergence in archaeal chromosomal proteins and Chromo-like domains from bacteria and eukaryotes.Scientific reports · 2018Article
- Structural basis of transcription initiation by RNA polymerase II.Nature reviews. Molecular cell biology · 2015Review
- Expression quantitative trait loci in long non-coding RNA ZNRD1-AS1 influence cervical cancer development.American journal of cancer research · 2015Article
- Structural insights into transcription initiation by RNA polymerase II.Trends in biochemical sciences · 2013Review
- Host and viral transcriptional regulators in Sulfolobus: an overview.Extremophiles : life under extreme conditions · 2013Review
- Functional analysis of archaeal MBF1 by complementation studies in yeast.Biology direct · 2011Article
- Structure of the C-terminal domain of transcription factor IIB from Trypanosoma brucei.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Solution structure of ribosomal protein L40E, a unique C4 zinc finger protein encoded by archaeon Sulfolobus solfataricus.Protein science : a publication of the Protein Society · 2008Article
- The central cell plays a critical role in pollen tube guidance in Arabidopsis.The Plant cell · 2007Article
- TFIIB and the regulation of transcription by RNA polymerase II.Chromosoma · 2007Review
- The positions of TFIIF and TFIIE in the RNA polymerase II transcription preinitiation complex.Nature structural & molecular biology · 2007Article
- A TFIIB-like protein is indispensable for spliced leader RNA gene transcription in Trypanosoma brucei.Nucleic acids research · 2006Article
- Modulation of zinc- and cobalt-binding affinities through changes in the stability of the zinc ribbon protein L36.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2005Article
- Structure and mechanism of the RNA polymerase II transcription machinery.Nature structural & molecular biology · 2004Review
- A nonconserved surface of the TFIIB zinc ribbon domain plays a direct role in RNA polymerase II recruitment.Molecular and cellular biology · 2004Article
- Probing Zn2+-binding effects on the zinc-ribbon domain of human general transcription factor TFIIB.The Biochemical journal · 2004Article
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5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transcription factor IIB (TFIIB) is an essential component in the formation of the transcription initiation complex in eucaryal and archaeal transcription. TFIIB interacts with a promoter complex containing the TATA-binding protein (TBP) to facilitate interaction with RNA polymerase II (RNA pol II) and the associated transcription factor IIF (TFIIF). TFIIB contains a zinc-binding motif near the N-terminus that is directly involved in the interaction with RNA pol II/TFIIF and plays a crucial role in selecting the transcription initiation site. The solution structure of the N-terminal residues 2-59 of human TFIIB was determined by multidimensional NMR spectroscopy. The structure consists of a nearly tetrahedral Zn(Cys)3(His)1 site confined by type I and "rubredoxin" turns, three antiparallel beta-strands, and disordered loops. The structure is similar to the reported zinc-ribbon motifs in several transcription-related proteins from archaea and eucarya, including Pyrococcus furiosus transcription factor B (PfTFB), human and yeast transcription factor IIS (TFIIS), and Thermococcus celer RNA polymerase II subunit M (TcRPOM). The zinc-ribbon structure of TFIIB, in conjunction with the biochemical analyses, suggests that residues on the beta-sheet are involved in the interaction with RNA pol II/TFIIF, while the zinc-binding site may increase the stability of the beta-sheet.
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