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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

หน่วยงาน Nanyang Technological University, Singapore

รายละเอียด

ชื่อเรื่อง : Novel zinc finger motif in the basal transcriptional machinery : three-dimensional NMR studies of the nucleic acid binding domain of transcriptional elongation factor TFIIS
นักวิจัย : Qian, Xiuqi , Gozani, Shai N. , Yoon, Ho Sup , Jeon, Choon Ju , Agarwal, Kan , Weiss, Michael A.
คำค้น : DRNTU::Science::Biological sciences::Biochemistry.
หน่วยงาน : Nanyang Technological University, Singapore
ผู้ร่วมงาน : -
ปีพิมพ์ : 2536
อ้างอิง : 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. , http://hdl.handle.net/10220/7481 , http://dx.doi.org/10.1021/bi00089a010
ที่มา : -
ความเชี่ยวชาญ : -
ความสัมพันธ์ : Biochemistry
ขอบเขตของเนื้อหา : -
บทคัดย่อ/คำอธิบาย :

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.

บรรณานุกรม :
Qian, Xiuqi , Gozani, Shai N. , Yoon, Ho Sup , Jeon, Choon Ju , Agarwal, Kan , Weiss, Michael A. . (2536). Novel zinc finger motif in the basal transcriptional machinery : three-dimensional NMR studies of the nucleic acid binding domain of transcriptional elongation factor TFIIS.
    กรุงเทพมหานคร : Nanyang Technological University, Singapore.
Qian, Xiuqi , Gozani, Shai N. , Yoon, Ho Sup , Jeon, Choon Ju , Agarwal, Kan , Weiss, Michael A. . 2536. "Novel zinc finger motif in the basal transcriptional machinery : three-dimensional NMR studies of the nucleic acid binding domain of transcriptional elongation factor TFIIS".
    กรุงเทพมหานคร : Nanyang Technological University, Singapore.
Qian, Xiuqi , Gozani, Shai N. , Yoon, Ho Sup , Jeon, Choon Ju , Agarwal, Kan , Weiss, Michael A. . "Novel zinc finger motif in the basal transcriptional machinery : three-dimensional NMR studies of the nucleic acid binding domain of transcriptional elongation factor TFIIS."
    กรุงเทพมหานคร : Nanyang Technological University, Singapore, 2536. Print.
Qian, Xiuqi , Gozani, Shai N. , Yoon, Ho Sup , Jeon, Choon Ju , Agarwal, Kan , Weiss, Michael A. . Novel zinc finger motif in the basal transcriptional machinery : three-dimensional NMR studies of the nucleic acid binding domain of transcriptional elongation factor TFIIS. กรุงเทพมหานคร : Nanyang Technological University, Singapore; 2536.