STRUCTURE OF A NEW NUCLEIC-ACID-BINDING MOTIF IN EUKARYOTIC TRANSCRIPTIONAL ELONGATION-FACTOR TFIIS

Article

关键词: RNA POLYMERASE-II;    ZINC FINGER;    CRYSTAL-STRUCTURE;    GLUCOCORTICOID RECEPTOR;    DNA RECOGNITION;    DOMAINS;    PROTEIN;    COMPLEX;    SUBUNIT;    BLOCK;   

DOI  :  10.1038/365277a0

来源: SCIE

【 摘 要 】

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 provides 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 eukaryotic 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 alpha-helix, this structure consists of a three-stranded beta-sheet. Analogous Cys4, structural motifs may occur in other proteins involved in DNA or RNA transactions22-24, including RNAPII itself25. This new structure, designated the Zn ribbon, extends the repertoire of Zn-mediated peptide architectures26 and highlights the growing recognition of the beta-sheet as a motif of nucleic-acid recognition27,28.

【 授权许可】

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