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Structure of a (Cys 3 His) zinc ribbon, a ubiquitous motif in archaeal and eucaryal transcription
Author(s) -
Chen HungTa,
Legault Pascale,
Glushka John,
Omichinski James G.,
Scott Robert A.
Publication year - 2000
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.9.9.1743
Subject(s) - transcription factor ii b , transcription factor ii f , transcription factor ii a , transcription factor ii d , general transcription factor , rna polymerase ii holoenzyme , transcription factor ii e , rna polymerase ii , transcription preinitiation complex , biology , transcription factor , rna polymerase , microbiology and biotechnology , chemistry , genetics , promoter , rna , gene , gene expression
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 ( Tc RPOM). 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.