Nucleotide sequence of the staphylocoagulase gene: Its unique COOH-terminal 8 tandem repeats

Shigenori Kaida, Toshiyuki Miyata, Yukio Yoshizawa, Shun-Ichiro Kawabata, Takashi Morita, Hideo Igarashi, Sadaaki Iwanaga

研究成果: ジャーナルへの寄稿記事

49 引用 (Scopus)

抄録

The entire staphylocoagulase gene of Staphylococcus aureus strain BB was cloned on a MboI restriction endonuclease fragment inserted into pAT153 plasmid vector. The staphylocoagulase was expressed in Escherichia coli, as judged by the formation of a fibrin halo on an agar plate containing rabbit plasma and bovine fibrinogen. We have determined the complete nucleotide sequence of the staphylocoagulase gene by the dideoxynucleotide chain termination method. The deduced amino acid sequence consisted of 715 residues including a signal peptide of 26 residues. Therefore, the predicted molecular weight of the mature protein was 77,337. This sequence was corroborated by reference to the amino acid compositions .of 30 lysyl endopeptidase peptides and the sequences of 12 of these peptides isolated from the purified staphylocoagulase. The 5′-flanking region was found to contain a putative Shine-Dalgarno sequence and a putative "- 10", element for transcription. The COOH-terminal stretch of 216 amino acids of staphylocoagulase was composed of 8 tandem repeats each consisting of 27 amino acid residues. The amino acid sequence of staphylocoagulase derived from strain BB showed 57 % identity with that of the chymotryptic 43-kDa fragment of staphylocoagulase isolated previously from strain 213 (Kawabata, S., Miyata, To., Morita, T., Miyata, Ta., Iwanaga, S., & Igarashi, H. (1986) J. Biol. Chem. 261, 527-531).

元の言語英語
ページ(範囲)1177-1186
ページ数10
ジャーナルJournal of biochemistry
102
発行部数5
DOI
出版物ステータス出版済み - 1 1 1987

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Tandem Repeat Sequences
Coagulase
Nucleotides
Genes
Amino Acids
lysyl endopeptidase
Amino Acid Sequence
Dideoxynucleotides
Peptides
5' Flanking Region
DNA Restriction Enzymes
Transcription
Protein Sorting Signals
Fibrin
Fibrinogen
Escherichia coli
Agar
Staphylococcus aureus
Plasmids
Molecular Weight

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

これを引用

Nucleotide sequence of the staphylocoagulase gene : Its unique COOH-terminal 8 tandem repeats. / Kaida, Shigenori; Miyata, Toshiyuki; Yoshizawa, Yukio; Kawabata, Shun-Ichiro; Morita, Takashi; Igarashi, Hideo; Iwanaga, Sadaaki.

:: Journal of biochemistry, 巻 102, 番号 5, 01.01.1987, p. 1177-1186.

研究成果: ジャーナルへの寄稿記事

Kaida, Shigenori ; Miyata, Toshiyuki ; Yoshizawa, Yukio ; Kawabata, Shun-Ichiro ; Morita, Takashi ; Igarashi, Hideo ; Iwanaga, Sadaaki. / Nucleotide sequence of the staphylocoagulase gene : Its unique COOH-terminal 8 tandem repeats. :: Journal of biochemistry. 1987 ; 巻 102, 番号 5. pp. 1177-1186.
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abstract = "The entire staphylocoagulase gene of Staphylococcus aureus strain BB was cloned on a MboI restriction endonuclease fragment inserted into pAT153 plasmid vector. The staphylocoagulase was expressed in Escherichia coli, as judged by the formation of a fibrin halo on an agar plate containing rabbit plasma and bovine fibrinogen. We have determined the complete nucleotide sequence of the staphylocoagulase gene by the dideoxynucleotide chain termination method. The deduced amino acid sequence consisted of 715 residues including a signal peptide of 26 residues. Therefore, the predicted molecular weight of the mature protein was 77,337. This sequence was corroborated by reference to the amino acid compositions .of 30 lysyl endopeptidase peptides and the sequences of 12 of these peptides isolated from the purified staphylocoagulase. The 5′-flanking region was found to contain a putative Shine-Dalgarno sequence and a putative {"}- 10{"}, element for transcription. The COOH-terminal stretch of 216 amino acids of staphylocoagulase was composed of 8 tandem repeats each consisting of 27 amino acid residues. The amino acid sequence of staphylocoagulase derived from strain BB showed 57 {\%} identity with that of the chymotryptic 43-kDa fragment of staphylocoagulase isolated previously from strain 213 (Kawabata, S., Miyata, To., Morita, T., Miyata, Ta., Iwanaga, S., & Igarashi, H. (1986) J. Biol. Chem. 261, 527-531).",
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