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

Makoto Kimura, Junko Kimura, Reiner Zierer

研究成果: ジャーナルへの寄稿 › 記事

6 引用 (Scopus)

抄録

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 Mrof 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.

元の言語英語
ページ（範囲）208-212
ページ数5
ジャーナルFEBS Letters
巻175
発行部数2
DOI
出版物ステータス出版済み - 10 1 1984

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Clostridium
DNA-Binding Proteins
Geobacillus stearothermophilus
glycyl-phenylalanyl-glycine
Amino Acids
Escherichia coli
Amino Acid Sequence
Thermoplasma
Bacilli
Protein C
Staphylococcus
Pseudomonas aeruginosa
Digestion
Proteins
Peptide Hydrolases
Degradation
Peptides
Molecules

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

これを引用

The primary structure of the DNA-binding protein II from Clostridium pasteurianum. / Kimura, Makoto; Kimura, Junko; Zierer, Reiner.

：: FEBS Letters, 巻 175, 番号 2, 01.10.1984, p. 208-212.

研究成果: ジャーナルへの寄稿 › 記事

Kimura, M, Kimura, J & Zierer, R 1984, 'The primary structure of the DNA-binding protein II from Clostridium pasteurianum', FEBS Letters, 巻. 175, 番号 2, pp. 208-212. https://doi.org/10.1016/0014-5793(84)80738-3
Kimura M, Kimura J, Zierer R. The primary structure of the DNA-binding protein II from Clostridium pasteurianum. FEBS Letters. 1984 10 1;175(2):208-212. https://doi.org/10.1016/0014-5793(84)80738-3
Kimura, Makoto ; Kimura, Junko ; Zierer, Reiner. / The primary structure of the DNA-binding protein II from Clostridium pasteurianum. ：: FEBS Letters. 1984 ; 巻 175, 番号 2. pp. 208-212.
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abstract = "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 Mrof 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.",
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N2 - 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 Mrof 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.

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