The complete primary structure of ribosomal proteins L1, L14, L15, L23, L24 and L29 from Bacillus stearothermophilus

Makoto KIMURA, Junko KIMURA, Keith ASHMAN

研究成果: ジャーナルへの寄稿記事

49 引用 (Scopus)

抄録

The amino acid sequences of ribosomal proteins L1, L14, L15, L23, L24 and L29 from Bacillus stearothermophilus have been completely determined. This has been achieved by sequence analyses of peptides derived from enzymatic digestions of the proteins with trypsin, chymotrypsin, pepsin, Staphylococcus aureus protease, and Armillaria mellea protease as well as by chemical cleavage with hydroxylamine and cyanogen bromide. Based on the primary structures of the six proteins, their secondary structures were predicted using four different computer prediction programs. A comparison of the amino acid sequences of the studied proteins from B. stearothermophilus with the homologous proteins from Escherichia coli revealed that in four proteins (L1, L15, L24 and L29) between 40–50% of the residue in the sequences are identical, whereas this value is significantly higher (69%) for L14 and lower (28%) for L23. The distribution of those amino acid residues which are identical in the corresponding proteins from the two bacteria is not random along the protein chain: some regions are highly conserved whereas others are not. This finding indicates that the regions which are conserved during evolution are important for the spatial structure and/or function of the protein.

元の言語英語
ページ(範囲)491-497
ページ数7
ジャーナルEuropean Journal of Biochemistry
150
発行部数3
DOI
出版物ステータス出版済み - 8 1985

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Geobacillus stearothermophilus
Bacilli
Amino Acid Sequence
Armillaria
Proteins
Peptide Hydrolases
Secondary Protein Structure
Amino Acids
Cyanogen Bromide
Hydroxylamine
Pepsin A
Escherichia coli Proteins
Protein Sequence Analysis
Proteolysis
Staphylococcus aureus
Software
Bacteria
ribosomal protein L1
ribosomal protein L14
Peptides

All Science Journal Classification (ASJC) codes

  • Biochemistry

これを引用

The complete primary structure of ribosomal proteins L1, L14, L15, L23, L24 and L29 from Bacillus stearothermophilus. / KIMURA, Makoto; KIMURA, Junko; ASHMAN, Keith.

:: European Journal of Biochemistry, 巻 150, 番号 3, 08.1985, p. 491-497.

研究成果: ジャーナルへの寄稿記事

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abstract = "The amino acid sequences of ribosomal proteins L1, L14, L15, L23, L24 and L29 from Bacillus stearothermophilus have been completely determined. This has been achieved by sequence analyses of peptides derived from enzymatic digestions of the proteins with trypsin, chymotrypsin, pepsin, Staphylococcus aureus protease, and Armillaria mellea protease as well as by chemical cleavage with hydroxylamine and cyanogen bromide. Based on the primary structures of the six proteins, their secondary structures were predicted using four different computer prediction programs. A comparison of the amino acid sequences of the studied proteins from B. stearothermophilus with the homologous proteins from Escherichia coli revealed that in four proteins (L1, L15, L24 and L29) between 40–50{\%} of the residue in the sequences are identical, whereas this value is significantly higher (69{\%}) for L14 and lower (28{\%}) for L23. The distribution of those amino acid residues which are identical in the corresponding proteins from the two bacteria is not random along the protein chain: some regions are highly conserved whereas others are not. This finding indicates that the regions which are conserved during evolution are important for the spatial structure and/or function of the protein.",
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