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Novel zinc finger motif in the basal transcriptional machinery : three-dimensional NMR studies of the nucleic acid binding domain of transcriptional elongation factor TFIIS

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Novel zinc finger motif in the basal transcriptional machinery : three-dimensional NMR studies of the nucleic acid binding domain of transcriptional elongation factor TFIIS

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dc.contributor.author Qian, Xiuqi
dc.contributor.author Gozani, Shai N.
dc.contributor.author Yoon, Ho Sup
dc.contributor.author Jeon, Choon Ju
dc.contributor.author Agarwal, Kan
dc.contributor.author Weiss, Michael A.
dc.date.accessioned 2012-01-26T03:14:46Z
dc.date.available 2012-01-26T03:14:46Z
dc.date.copyright 1993
dc.date.issued 2012-01-26
dc.identifier.citation 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.
dc.identifier.uri http://hdl.handle.net/10220/7481
dc.description.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.
dc.language.iso en
dc.relation.ispartofseries Biochemistry
dc.rights © 1993 American Chemical Society.
dc.subject DRNTU::Science::Biological sciences::Biochemistry.
dc.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
dc.type Journal Article
dc.contributor.school School of Biological Sciences
dc.identifier.doi http://dx.doi.org/10.1021/bi00089a010

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