Primary Structure of Escherichia coli Ribosomal Protein S1 and Features of Its Functional Domains

Makoto Kimura, Kirani FOULAKI, Alap‐Raman ‐R SUBRAMANIAN, Brigitte WITTMANN‐LIEBOLD

研究成果: ジャーナルへの寄稿記事

27 引用 (Scopus)

抄録

The complete covalent structure of ribosomal protein S1 of Eschericlziu coli has been determined and predictions made of its secondary structure. Protein S1 (E. coli MRE 600) is a single‐chain, acidic protein with 557 amino acid residues of the composition Asp43, Asn23, Thr25, Ser25, Glu60, Glnl4, Pro10, Gly48, Ala48, Val67, Met6, Ile30, Leu45, Tyr6, Phe17, His8, LYS43, Arg30, Trp7, Cys2 and an Mr, of 61159. The two ‐SH groups of S1 are located in the central region of the chain at positions 292 and 349, the latter being the reactive group whose modification results in the reported loss of the nucleic‐acid‐unfolding ability of S1, The central region also contains the majority of the tryptophan, histidine and methionine residues of S1 and is predicted to have a secondary structure dominated by β‐sheets and turns. A direct proof for the location of the nucleic‐acid‐binding domain of S1 in the central region has recently been obtained [Subramanian et al. (1981) Eur. J. Biochem. 119, 245‐249], The N‐terminal region of S1, which contains the ribosome‐binding domain has a relatively high predicted α‐helix content and no preponderance of basic amino acids. The facile trypsin‐sensitive site in S1 is located at Arg‐171, approximately at the border between the N‐terminal and central regions. The acidic and basic amino acids of S1 (32.8% of all residues) are distributed throughout the chain, often in small clusters of between two and six residues. The amino acid sequence of S1 contains three 24‐residue stretches with strong internal homology. Two of the stretches are located in the central, RNA‐binding region, suggesting a possible role in the RNA‐binding and helix‐destabilizing functions of S1. A fragment of Mr, 104 from the central region of S1 gives an anomalously high apparent Mr, by dodecylsulfate gel electrophoresis, indicating a stable structural element therein and accounting for the apparent high Mr, of S1 as determined by gel electrophoresis.

元の言語英語
ページ(範囲)37-53
ページ数17
ジャーナルEuropean Journal of Biochemistry
123
発行部数1
DOI
出版物ステータス出版済み - 1 1 1982

Fingerprint

Basic Amino Acids
Escherichia coli Proteins
Electrophoresis
Escherichia coli
Gels
Acidic Amino Acids
Amino Acids
Histidine
Tryptophan
Methionine
Amino Acid Sequence
Proteins
Chemical analysis
ribosomal protein S1

All Science Journal Classification (ASJC) codes

  • Biochemistry

これを引用

Primary Structure of Escherichia coli Ribosomal Protein S1 and Features of Its Functional Domains. / Kimura, Makoto; FOULAKI, Kirani; SUBRAMANIAN, Alap‐Raman ‐R; WITTMANN‐LIEBOLD, Brigitte.

:: European Journal of Biochemistry, 巻 123, 番号 1, 01.01.1982, p. 37-53.

研究成果: ジャーナルへの寄稿記事

Kimura, Makoto ; FOULAKI, Kirani ; SUBRAMANIAN, Alap‐Raman ‐R ; WITTMANN‐LIEBOLD, Brigitte. / Primary Structure of Escherichia coli Ribosomal Protein S1 and Features of Its Functional Domains. :: European Journal of Biochemistry. 1982 ; 巻 123, 番号 1. pp. 37-53.
@article{3ef1bd45b5e24a1b9a82dae2185a86ff,
title = "Primary Structure of Escherichia coli Ribosomal Protein S1 and Features of Its Functional Domains",
abstract = "The complete covalent structure of ribosomal protein S1 of Eschericlziu coli has been determined and predictions made of its secondary structure. Protein S1 (E. coli MRE 600) is a single‐chain, acidic protein with 557 amino acid residues of the composition Asp43, Asn23, Thr25, Ser25, Glu60, Glnl4, Pro10, Gly48, Ala48, Val67, Met6, Ile30, Leu45, Tyr6, Phe17, His8, LYS43, Arg30, Trp7, Cys2 and an Mr, of 61159. The two ‐SH groups of S1 are located in the central region of the chain at positions 292 and 349, the latter being the reactive group whose modification results in the reported loss of the nucleic‐acid‐unfolding ability of S1, The central region also contains the majority of the tryptophan, histidine and methionine residues of S1 and is predicted to have a secondary structure dominated by β‐sheets and turns. A direct proof for the location of the nucleic‐acid‐binding domain of S1 in the central region has recently been obtained [Subramanian et al. (1981) Eur. J. Biochem. 119, 245‐249], The N‐terminal region of S1, which contains the ribosome‐binding domain has a relatively high predicted α‐helix content and no preponderance of basic amino acids. The facile trypsin‐sensitive site in S1 is located at Arg‐171, approximately at the border between the N‐terminal and central regions. The acidic and basic amino acids of S1 (32.8{\%} of all residues) are distributed throughout the chain, often in small clusters of between two and six residues. The amino acid sequence of S1 contains three 24‐residue stretches with strong internal homology. Two of the stretches are located in the central, RNA‐binding region, suggesting a possible role in the RNA‐binding and helix‐destabilizing functions of S1. A fragment of Mr, 104 from the central region of S1 gives an anomalously high apparent Mr, by dodecylsulfate gel electrophoresis, indicating a stable structural element therein and accounting for the apparent high Mr, of S1 as determined by gel electrophoresis.",
author = "Makoto Kimura and Kirani FOULAKI and SUBRAMANIAN, {Alap‐Raman ‐R} and Brigitte WITTMANN‐LIEBOLD",
year = "1982",
month = "1",
day = "1",
doi = "10.1111/j.1432-1033.1982.tb06495.x",
language = "English",
volume = "123",
pages = "37--53",
journal = "FEBS Journal",
issn = "1742-464X",
publisher = "Wiley-Blackwell",
number = "1",

}

TY - JOUR

T1 - Primary Structure of Escherichia coli Ribosomal Protein S1 and Features of Its Functional Domains

AU - Kimura, Makoto

AU - FOULAKI, Kirani

AU - SUBRAMANIAN, Alap‐Raman ‐R

AU - WITTMANN‐LIEBOLD, Brigitte

PY - 1982/1/1

Y1 - 1982/1/1

N2 - The complete covalent structure of ribosomal protein S1 of Eschericlziu coli has been determined and predictions made of its secondary structure. Protein S1 (E. coli MRE 600) is a single‐chain, acidic protein with 557 amino acid residues of the composition Asp43, Asn23, Thr25, Ser25, Glu60, Glnl4, Pro10, Gly48, Ala48, Val67, Met6, Ile30, Leu45, Tyr6, Phe17, His8, LYS43, Arg30, Trp7, Cys2 and an Mr, of 61159. The two ‐SH groups of S1 are located in the central region of the chain at positions 292 and 349, the latter being the reactive group whose modification results in the reported loss of the nucleic‐acid‐unfolding ability of S1, The central region also contains the majority of the tryptophan, histidine and methionine residues of S1 and is predicted to have a secondary structure dominated by β‐sheets and turns. A direct proof for the location of the nucleic‐acid‐binding domain of S1 in the central region has recently been obtained [Subramanian et al. (1981) Eur. J. Biochem. 119, 245‐249], The N‐terminal region of S1, which contains the ribosome‐binding domain has a relatively high predicted α‐helix content and no preponderance of basic amino acids. The facile trypsin‐sensitive site in S1 is located at Arg‐171, approximately at the border between the N‐terminal and central regions. The acidic and basic amino acids of S1 (32.8% of all residues) are distributed throughout the chain, often in small clusters of between two and six residues. The amino acid sequence of S1 contains three 24‐residue stretches with strong internal homology. Two of the stretches are located in the central, RNA‐binding region, suggesting a possible role in the RNA‐binding and helix‐destabilizing functions of S1. A fragment of Mr, 104 from the central region of S1 gives an anomalously high apparent Mr, by dodecylsulfate gel electrophoresis, indicating a stable structural element therein and accounting for the apparent high Mr, of S1 as determined by gel electrophoresis.

AB - The complete covalent structure of ribosomal protein S1 of Eschericlziu coli has been determined and predictions made of its secondary structure. Protein S1 (E. coli MRE 600) is a single‐chain, acidic protein with 557 amino acid residues of the composition Asp43, Asn23, Thr25, Ser25, Glu60, Glnl4, Pro10, Gly48, Ala48, Val67, Met6, Ile30, Leu45, Tyr6, Phe17, His8, LYS43, Arg30, Trp7, Cys2 and an Mr, of 61159. The two ‐SH groups of S1 are located in the central region of the chain at positions 292 and 349, the latter being the reactive group whose modification results in the reported loss of the nucleic‐acid‐unfolding ability of S1, The central region also contains the majority of the tryptophan, histidine and methionine residues of S1 and is predicted to have a secondary structure dominated by β‐sheets and turns. A direct proof for the location of the nucleic‐acid‐binding domain of S1 in the central region has recently been obtained [Subramanian et al. (1981) Eur. J. Biochem. 119, 245‐249], The N‐terminal region of S1, which contains the ribosome‐binding domain has a relatively high predicted α‐helix content and no preponderance of basic amino acids. The facile trypsin‐sensitive site in S1 is located at Arg‐171, approximately at the border between the N‐terminal and central regions. The acidic and basic amino acids of S1 (32.8% of all residues) are distributed throughout the chain, often in small clusters of between two and six residues. The amino acid sequence of S1 contains three 24‐residue stretches with strong internal homology. Two of the stretches are located in the central, RNA‐binding region, suggesting a possible role in the RNA‐binding and helix‐destabilizing functions of S1. A fragment of Mr, 104 from the central region of S1 gives an anomalously high apparent Mr, by dodecylsulfate gel electrophoresis, indicating a stable structural element therein and accounting for the apparent high Mr, of S1 as determined by gel electrophoresis.

UR - http://www.scopus.com/inward/record.url?scp=0020048339&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0020048339&partnerID=8YFLogxK

U2 - 10.1111/j.1432-1033.1982.tb06495.x

DO - 10.1111/j.1432-1033.1982.tb06495.x

M3 - Article

VL - 123

SP - 37

EP - 53

JO - FEBS Journal

JF - FEBS Journal

SN - 1742-464X

IS - 1

ER -