A DNA binding protein from the extreme thermophile Thermus thermophilus

FEBS Letters

Dijk, Jan¹  Grote, Mathias¹  Zierer, Rainer¹  Wilson, Keith¹ 

[1] Max-Planck-Institut für Molekulare Genetik, Abt. Wittmann, Ihnestrasse 63-73, D-1000 Berlin 33, Germany

关键词: Thermophile;    DNA binding protein;    Crystal;   

DOI  :  10.1016/0014-5793(86)80091-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A DNA binding protein was extracted and purified from Thermus thermophilus HB8 grown at 75°C. The protein has an M _r of 10 000 and from the partial data available shows a weak but clear sequence homology to the DNA binding protein II family. The protein is able to bind to DNA, and can also bind to RNA and to ribosomes. It affects the melting profile of the nucleic acids. From circular dichroic spectra an α-helix content of 32% and β-sheet of 40% are estimated. The proton NMR spectrum indicates a well folded tertiary structure. Upon binding of oligonucleotides pronounced changes in the NMR spectrum of the protein can be seen. Comparable changes are observed in circular dichroic spectra of protein-oligonucleotide complexes. Hexagonal crystals, which diffract to at least 3 Å, of the DNA binding protein have been obtained using ammonium sulphate as precipitant. The space group is P6₂22, with cell dimensions a = b = 62.9 Å and c = 110.6 Å.

【 授权许可】

Unknown