The amino acid sequence of two small ribosomal proteins from Bacillus stearothermophilus

Isao Tanaka, Makoto Kimura, Junko Kimura, Jan Dijk

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

The low-Mr proteins (tentatively called protein I and II) were purified from 2 M NaCl extracts of the Bacillus stearothermophilus ribosome. Their amino acid sequences have been determined from the peptides obtained by digestion with trypsin, chymotrypsin, and pepsin, and by cleavage with CNBr, using the micro-DABITC/PITC double-coupling method [FEBS Lett. (1978) 93, 205-214]. Protein I contains 56 residues and has an Mr of 6514. Protein II had 37 residues with an Mr of 4361. The amino acid sequence of protein I shows significant similarity to L32 from E. coli, whereas that of protein II is slightly, if at all, related to ribosomal protein L34 from E. coli.

Original languageEnglish
Pages (from-to)343-346
Number of pages4
JournalFEBS Letters
Volume166
Issue number2
DOIs
Publication statusPublished - Jan 30 1984

Fingerprint

Geobacillus stearothermophilus
Ribosomal Proteins
Bacilli
Amino Acid Sequence
Amino Acids
Proteins
Pepsin A
Escherichia coli Proteins
Ribosomes
Escherichia coli
Digestion
Peptides

All Science Journal Classification (ASJC) codes

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

Cite this

The amino acid sequence of two small ribosomal proteins from Bacillus stearothermophilus. / Tanaka, Isao; Kimura, Makoto; Kimura, Junko; Dijk, Jan.

In: FEBS Letters, Vol. 166, No. 2, 30.01.1984, p. 343-346.

Research output: Contribution to journalArticle

Tanaka, Isao ; Kimura, Makoto ; Kimura, Junko ; Dijk, Jan. / The amino acid sequence of two small ribosomal proteins from Bacillus stearothermophilus. In: FEBS Letters. 1984 ; Vol. 166, No. 2. pp. 343-346.
@article{e37cf45c21394fcfb0c9b982a5638cb9,
title = "The amino acid sequence of two small ribosomal proteins from Bacillus stearothermophilus",
abstract = "The low-Mr proteins (tentatively called protein I and II) were purified from 2 M NaCl extracts of the Bacillus stearothermophilus ribosome. Their amino acid sequences have been determined from the peptides obtained by digestion with trypsin, chymotrypsin, and pepsin, and by cleavage with CNBr, using the micro-DABITC/PITC double-coupling method [FEBS Lett. (1978) 93, 205-214]. Protein I contains 56 residues and has an Mr of 6514. Protein II had 37 residues with an Mr of 4361. The amino acid sequence of protein I shows significant similarity to L32 from E. coli, whereas that of protein II is slightly, if at all, related to ribosomal protein L34 from E. coli.",
author = "Isao Tanaka and Makoto Kimura and Junko Kimura and Jan Dijk",
year = "1984",
month = "1",
day = "30",
doi = "10.1016/0014-5793(84)80109-X",
language = "English",
volume = "166",
pages = "343--346",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "2",

}

TY - JOUR

T1 - The amino acid sequence of two small ribosomal proteins from Bacillus stearothermophilus

AU - Tanaka, Isao

AU - Kimura, Makoto

AU - Kimura, Junko

AU - Dijk, Jan

PY - 1984/1/30

Y1 - 1984/1/30

N2 - The low-Mr proteins (tentatively called protein I and II) were purified from 2 M NaCl extracts of the Bacillus stearothermophilus ribosome. Their amino acid sequences have been determined from the peptides obtained by digestion with trypsin, chymotrypsin, and pepsin, and by cleavage with CNBr, using the micro-DABITC/PITC double-coupling method [FEBS Lett. (1978) 93, 205-214]. Protein I contains 56 residues and has an Mr of 6514. Protein II had 37 residues with an Mr of 4361. The amino acid sequence of protein I shows significant similarity to L32 from E. coli, whereas that of protein II is slightly, if at all, related to ribosomal protein L34 from E. coli.

AB - The low-Mr proteins (tentatively called protein I and II) were purified from 2 M NaCl extracts of the Bacillus stearothermophilus ribosome. Their amino acid sequences have been determined from the peptides obtained by digestion with trypsin, chymotrypsin, and pepsin, and by cleavage with CNBr, using the micro-DABITC/PITC double-coupling method [FEBS Lett. (1978) 93, 205-214]. Protein I contains 56 residues and has an Mr of 6514. Protein II had 37 residues with an Mr of 4361. The amino acid sequence of protein I shows significant similarity to L32 from E. coli, whereas that of protein II is slightly, if at all, related to ribosomal protein L34 from E. coli.

UR - http://www.scopus.com/inward/record.url?scp=0021773222&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021773222&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(84)80109-X

DO - 10.1016/0014-5793(84)80109-X

M3 - Article

VL - 166

SP - 343

EP - 346

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 2

ER -