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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.
| 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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