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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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
}
TY - JOUR
T1 - The primary structure of the DNA-binding protein II from Clostridium pasteurianum
AU - Kimura, Makoto
AU - Kimura, Junko
AU - Zierer, Reiner
PY - 1984/10/1
Y1 - 1984/10/1
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.
AB - 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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UR - http://www.scopus.com/inward/citedby.url?scp=0021505334&partnerID=8YFLogxK
U2 - 10.1016/0014-5793(84)80738-3
DO - 10.1016/0014-5793(84)80738-3
M3 - Article
C2 - 6541161
AN - SCOPUS:0021505334
VL - 175
SP - 208
EP - 212
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 2
ER -