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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.
| 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. |
| Author: | Qian, Xiuqi.; Gozani, Shai N.; Yoon, Ho Sup.; Jeon, Choon Ju.; Agarwal, Kan.; Weiss, Michael A. |
| Copyright year: | 1993 |
| 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. |
| Subject: | DRNTU::Science::Biological sciences::Biochemistry. |
| Type: | Journal Article |
| Series/ Journal Title: | Biochemistry |
| School: | School of Biological Sciences |
| Rights: | © 1993 American Chemical Society. |
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