The primary structure of the DNA‐binding protein II from Clostridium pasteurianum

FEBS Letters

Kimura, Makoto¹  Zierer, Reiner¹  Kimura, Junko¹ 

[1] Max-Planck-Institut für Molekulare Genetik, Abteilung Wittmann, Ihnestrasse 63-73, D-1000 Berlin 33 (Dahlem), Germany

关键词: Amino acid sequence;    DNA-binding protein II;    Protein evolution;    Clostridium pasteurianum;   

DOI  :  10.1016/0014-5793(84)80738-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The complete amino acid sequence of the Clostridium pasteurianum DNA-binding protein II (DNAb-II) has been determined. The molecule contains 91 amino acid residues and has an M _rof 10133. Sequence data were obtained from manual Edman degradation, using the DABITC/PITC double-coupling of the tryptic, peptic, chymotryptic and Staphylococcus protease peptides. A comparison of the amino acid sequence of the C. pasteurianum DNAb-II with those of the DNAb-II from Escherichia coli, Bacillus stearothermophilus, Thermoplasma acidophilum and Pseudomonas aeruginosa shows that the C. pasteurianum protein is more homologous to that of B. stearothermophilus (60%) than to that of E. coli (45%). All DNAb-II proteins have identical sequences Gly-Phe-Gly-X-Phe at positions 46–50 and Arg-Asn-Pro-X-Thr at positions 61–65.

【 授权许可】

Unknown