The hyperthermophile chromsomal protein Sac7d sharply kinks DNA

Howard Robinson, Yi Gui Gao, Bradford S. McCrary, Stephen P. Edmondson, John W. Shriver, Andrew H.J. Wang

研究成果: 雜誌貢獻文章同行評審

166 引文 斯高帕斯(Scopus)

摘要

The proteins Sac7d and Sso7d belong to a class of small chromosomal proteins from the hyperthermophilic archaeon Sulfolobus acidocaldarius and S. solfactaricus, respectively. These proteins are extremely stable to heat, acid and chemical agents. Sac7d binds to DNA without any particular sequence preference and thereby increases its melting temperature by ~40°C (ref. 4). We have now solved and refined the crystal structure of Sac7d in complex with two DNA sequences to high resolution. The structures are examples of a nonspecific DNA-binding protein bound to DNA, and reveal that Sac7d binds in the minor groove, causing a sharp kinking of the DNA helix that is more marked than that induced by any sequence-specific DNA-binding proteins. The kink results from the intercalation of specific hydrophobic side chains of Sac7d into the DNA structure, but without causing any significant distortion of the protein structure relative to the uncomplexed protein in solution.

原文英語
頁(從 - 到)202-205
頁數4
期刊Nature
392
發行號6672
DOIs
出版狀態已發佈 - 3月 12 1998
對外發佈

ASJC Scopus subject areas

  • 多學科

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