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Structure of a new nucleic-acid-binding motif in eukaryotic transcriptional elongation factor TFIIS

หน่วยงาน Nanyang Technological University, Singapore

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ชื่อเรื่อง : Structure of a new nucleic-acid-binding motif in eukaryotic transcriptional elongation factor TFIIS
นักวิจัย : Qian, Xiuqu , Jeon, Choon Ju , Yoon, Ho Sup , Agarwal, Kan , Weiss, Michael A.
คำค้น : DRNTU::Science::Biological sciences.
หน่วยงาน : Nanyang Technological University, Singapore
ผู้ร่วมงาน : -
ปีพิมพ์ : 2536
อ้างอิง : Qian, X., Jeon, C., Yoon, H., Agarwal, K., & Weiss, M.A.(1993). Structure of a new nucleic-acid-binding motif in eukaryotic transcriptional elongation factor TFIIS. Nature, 365, 277-279. , http://hdl.handle.net/10220/7719 , http://dx.doi.org/10.1038/365277a0
ที่มา : -
ความเชี่ยวชาญ : -
ความสัมพันธ์ : Nature
ขอบเขตของเนื้อหา : -
บทคัดย่อ/คำอธิบาย :

Transcriptional elongation involves dynamic interactions among RNA polymerase and single-stranded and double stranded nucleic acids in the ternary complex1–4. In prokaryotes its regulation pro-vides an important mechanism of genetic control1. Analogous eukaryotic mechanisms are not well understood5, but may control expression of proto-oncogenes6,7 and viruses, including the human immunodeficiency virus HIV-1 (ref. 8). The highly conserved euk-aryotic transcriptional elongation factor TFIIS9 enables RNA polymerase II (RNAPII) to read though pause or termination sites, nucleosomes and sequence-specific DNA-binding proteins10–14. Two distinct domains of human TFIIS, which bind RNAPII and nucleic acids, regulate read-through10 and possibly nascent transcript cleavage11–15. Here we describe the three-dimensional NMR16 structure of a Cys4 nucleic-acid-binding domain from human TFIIS9,10. Unlike previously characterized zinc modules17–21, which contain an α-helix, this structure consists of a three-stranded β-sheet. Analogous Cys4 structural motifs may occur in other proteins involved in DNA or RNA trans-actions22–24, including RNAPII itself25. This new structure, desig-nated the Zn ribbon, extends the repertoire of Zn-mediated peptide architectures26 and highlights the growing recognition of the β-sheet as a motif of nucleic-acid recognition27,28.

บรรณานุกรม :
Qian, Xiuqu , Jeon, Choon Ju , Yoon, Ho Sup , Agarwal, Kan , Weiss, Michael A. . (2536). Structure of a new nucleic-acid-binding motif in eukaryotic transcriptional elongation factor TFIIS.
    กรุงเทพมหานคร : Nanyang Technological University, Singapore.
Qian, Xiuqu , Jeon, Choon Ju , Yoon, Ho Sup , Agarwal, Kan , Weiss, Michael A. . 2536. "Structure of a new nucleic-acid-binding motif in eukaryotic transcriptional elongation factor TFIIS".
    กรุงเทพมหานคร : Nanyang Technological University, Singapore.
Qian, Xiuqu , Jeon, Choon Ju , Yoon, Ho Sup , Agarwal, Kan , Weiss, Michael A. . "Structure of a new nucleic-acid-binding motif in eukaryotic transcriptional elongation factor TFIIS."
    กรุงเทพมหานคร : Nanyang Technological University, Singapore, 2536. Print.
Qian, Xiuqu , Jeon, Choon Ju , Yoon, Ho Sup , Agarwal, Kan , Weiss, Michael A. . Structure of a new nucleic-acid-binding motif in eukaryotic transcriptional elongation factor TFIIS. กรุงเทพมหานคร : Nanyang Technological University, Singapore; 2536.