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|Title:||Novel zinc finger motif in the basal transcriptional machinery : three-dimensional NMR studies of the nucleic acid binding domain of transcriptional elongation factor TFIIS||Authors:||Gozani, Shai N.
Weiss, Michael A.
Yoon, Ho Sup
Jeon, Choon Ju
|Keywords:||DRNTU::Science::Biological sciences::Biochemistry||Issue Date:||1993||Source:||Qian, X., Gozani, S. N., Yoon, H., Jeon, C., Agarwal, K., & Weiss, M. A. (1993). Novel zinc finger motif in the basal transcriptional machinery: Three-dimensional NMR studies of the nucleic acid binding domain of transcriptional elongation factor TFIIS. Biochemistry, 32(38), 9944-9959.||Series/Report no.:||Biochemistry||Abstract:||Transcriptional elongation provides a key control point in the regulation of eukaryotic gene expression. Here we describe homonuclear and lSN-heteronuclear 3D NMR studies of the nucleic acid binding domain of human transcriptional elongation factor TFIIS. This domain contains a Cys4 ZnZ+- binding site with no homology to previously characterized Cys4, Cysa, or Cysz-His2 Zn fingers. Complete lH and I5N NMR resonance assignment of a 50-residue TFIIS peptideZnz+ complex is obtained. Its solution structure, as determined by distance geometry/simulated annealing (DG/SA) calculations, exhibits a novel three-stranded antiparallel p-sheet (designated the Zn ribbon). Analogous sequence motifs occur in a wide class of proteins involved in RNA or DNA transactions, including human basal transcriptional initiation factor TFIIE. A three-dimensional model of the TFIIE Cys4 domain is obtained by DG-based homology modeling. The role of the TFIIS Zn ribbon in the control of eukaryotic transcriptional elongation is discussed.||URI:||https://hdl.handle.net/10356/94285
|DOI:||10.1021/bi00089a010||Rights:||© 1993 American Chemical Society.||Fulltext Permission:||none||Fulltext Availability:||No Fulltext|
|Appears in Collections:||SBS Journal Articles|
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