THE PRIMARY STRUCTURE OF DNA-BINDING PROTEIN-II FROM THE EXTREME THERMOPHILIC BACTERIUM THERMUS-THERMOPHILUS

被引：13

作者：

ZIERER, R ^{[1
]}

CHOLI, D ^{[1
]}

机构：

[1] MAX PLANCK INST MOLEC GENET,WITTMANN ABT,W-1000 BERLIN 33,GERMANY

来源：

FEBS LETTERS | 1990年 / 273卷 / 1-2期

关键词：

DNA-binding protein II; Homology; Primary structure; Thermophilic bacteria;

D O I：

10.1016/0014-5793(90)81050-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The primary structure of DNA binding protein II (DNA bp II) from the extreme thermophilic bacterium Thermus thermophilus has been established by combination of manual and automated techniques. The protein has 95 residues and a molecular mass of 11843. Comparison of the primary structure with the known sequence data of DNA bp II from Clostridium pasteurineum, Baccillus stearothermophilus, Escherichia coli, Rhizobium meliloti, Anabena, Thermoplasma acidophilum, Pseudomonas aeruginosa and Bacillus caldolyticus reveals a clear homology among these small basic proteins. In particular, two short sequences in the middle and C-terminal part of the proteins (residues N-Gly-Phe-Gly-X-Phe and Pro-X-Thr at positions 46-51 and 63-65, respectively) are completely conserved. © 1990.

引用

页码：59 / 62

页数：4

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