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dc.contributor.authorGozani, Shai N.en
dc.contributor.authorWeiss, Michael A.en
dc.contributor.authorQian, Xiuqien
dc.contributor.authorYoon, Ho Supen
dc.contributor.authorJeon, Choon Juen
dc.contributor.authorAgarwal, Kanen
dc.identifier.citationQian, 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.en
dc.description.abstractTranscriptional 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.en
dc.rights© 1993 American Chemical Society.en
dc.subjectDRNTU::Science::Biological sciences::Biochemistryen
dc.titleNovel zinc finger motif in the basal transcriptional machinery : three-dimensional NMR studies of the nucleic acid binding domain of transcriptional elongation factor TFIISen
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen
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