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Structure of a (Cys3His) zinc ribbon, a ubiquitous motif in archaeal and eucaryal transcription

Published online by Cambridge University Press:  05 October 2000

HUNG-TA CHEN ,
PASCALE LEGAULT ,
JOHN GLUSHKA ,
JAMES G. OMICHINSKI  and
ROBERT A. SCOTT
HUNG-TA CHEN
Affiliation:
Center for Metalloenzyme Studies, Chemistry Building, University of Georgia, Athens, Georgia 30602-2556 Department of Chemistry, Chemistry Building, University of Georgia, Athens, Georgia 30602-2556
PASCALE LEGAULT
Affiliation:
Department of Biochemistry and Molecular Biology, Life Sciences Building, University of Georgia, Athens, Georgia 30602-7229
JOHN GLUSHKA
Affiliation:
Complex Carbohydrate Research Center, 220 Riverbend Road, University of Georgia, Athens, Georgia 30602-4712
JAMES G. OMICHINSKI
Affiliation:
Department of Chemistry, Chemistry Building, University of Georgia, Athens, Georgia 30602-2556 Department of Biochemistry and Molecular Biology, Life Sciences Building, University of Georgia, Athens, Georgia 30602-7229
ROBERT A. SCOTT
Affiliation:
Center for Metalloenzyme Studies, Chemistry Building, University of Georgia, Athens, Georgia 30602-2556 Department of Chemistry, Chemistry Building, University of Georgia, Athens, Georgia 30602-2556 Department of Biochemistry and Molecular Biology, Life Sciences Building, University of Georgia, Athens, Georgia 30602-7229
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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 β-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 (Pf TFB), 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 β-sheet are involved in the interaction with RNA pol II/TFIIF, while the zinc-binding site may increase the stability of the β-sheet.

Keywords

human transcription factor IIBmultidimensional NMRtranscription preinitiation complexzinc ribbon
Type
Research Article
Information
Protein Science , Volume 9 , Issue 9 , September 2000 , pp. 1743 - 1752
Copyright
2000 The Protein Society

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