The complete amino acid sequence of ribosomal protein H-S11 from the archaebacterium Halobacterium marismortui

Evelyn Arndt, Gabriele Breithaupt, Makoto Kimura

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

The complete amino acid sequence of ribosomal protein H-S11 from the extremely halophilic archaebacterium Halobacterium marismortui is presented. This has been achieved by the sequence analysis of peptides derived by enzymatic digestions with trypsin, pepsin and Staphylococcus aureus protease, as well as by chemical cleavage with cyanogen bromide and o-iodosobenzoic acid. The protein consists of 155 amino acid residues and has a molecular mass of 17545 Da. Comparison of this sequence with other ribosomal proteins by the computer programmes RELATE and ALIGN showed that the C-terminal two-thirds of H-S11 is homologous to the eubacterial ribosomal protein S15 and that the N-terminal one-third of H-S11 is possibly related to the N-terminal region of the eubacterial ribosomal protein S8. To explain this finding, possible genetic events during evolution, e.g. fusion or splitting of genes, are discussed.

Original languageEnglish
Pages (from-to)227-234
Number of pages8
JournalFEBS Letters
Volume194
Issue number2
DOIs
Publication statusPublished - Jan 6 1986

Fingerprint

Haloarcula marismortui
Cyanogen Bromide
Ribosomal Proteins
Pepsin A
Archaea
Protein Sequence Analysis
Trypsin
Staphylococcus aureus
Digestion
Amino Acid Sequence
Peptide Hydrolases
Software
Amino Acids
Acids
Molecular mass
Genes
Computer program listings
Proteins
Fusion reactions
Peptides

All Science Journal Classification (ASJC) codes

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

Cite this

The complete amino acid sequence of ribosomal protein H-S11 from the archaebacterium Halobacterium marismortui. / Arndt, Evelyn; Breithaupt, Gabriele; Kimura, Makoto.

In: FEBS Letters, Vol. 194, No. 2, 06.01.1986, p. 227-234.

Research output: Contribution to journalArticle

Arndt, Evelyn ; Breithaupt, Gabriele ; Kimura, Makoto. / The complete amino acid sequence of ribosomal protein H-S11 from the archaebacterium Halobacterium marismortui. In: FEBS Letters. 1986 ; Vol. 194, No. 2. pp. 227-234.
@article{2692e1a898144ae4ba1aa59011dcac39,
title = "The complete amino acid sequence of ribosomal protein H-S11 from the archaebacterium Halobacterium marismortui",
abstract = "The complete amino acid sequence of ribosomal protein H-S11 from the extremely halophilic archaebacterium Halobacterium marismortui is presented. This has been achieved by the sequence analysis of peptides derived by enzymatic digestions with trypsin, pepsin and Staphylococcus aureus protease, as well as by chemical cleavage with cyanogen bromide and o-iodosobenzoic acid. The protein consists of 155 amino acid residues and has a molecular mass of 17545 Da. Comparison of this sequence with other ribosomal proteins by the computer programmes RELATE and ALIGN showed that the C-terminal two-thirds of H-S11 is homologous to the eubacterial ribosomal protein S15 and that the N-terminal one-third of H-S11 is possibly related to the N-terminal region of the eubacterial ribosomal protein S8. To explain this finding, possible genetic events during evolution, e.g. fusion or splitting of genes, are discussed.",
author = "Evelyn Arndt and Gabriele Breithaupt and Makoto Kimura",
year = "1986",
month = "1",
day = "6",
doi = "10.1016/0014-5793(86)80090-4",
language = "English",
volume = "194",
pages = "227--234",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "2",

}

TY - JOUR

T1 - The complete amino acid sequence of ribosomal protein H-S11 from the archaebacterium Halobacterium marismortui

AU - Arndt, Evelyn

AU - Breithaupt, Gabriele

AU - Kimura, Makoto

PY - 1986/1/6

Y1 - 1986/1/6

N2 - The complete amino acid sequence of ribosomal protein H-S11 from the extremely halophilic archaebacterium Halobacterium marismortui is presented. This has been achieved by the sequence analysis of peptides derived by enzymatic digestions with trypsin, pepsin and Staphylococcus aureus protease, as well as by chemical cleavage with cyanogen bromide and o-iodosobenzoic acid. The protein consists of 155 amino acid residues and has a molecular mass of 17545 Da. Comparison of this sequence with other ribosomal proteins by the computer programmes RELATE and ALIGN showed that the C-terminal two-thirds of H-S11 is homologous to the eubacterial ribosomal protein S15 and that the N-terminal one-third of H-S11 is possibly related to the N-terminal region of the eubacterial ribosomal protein S8. To explain this finding, possible genetic events during evolution, e.g. fusion or splitting of genes, are discussed.

AB - The complete amino acid sequence of ribosomal protein H-S11 from the extremely halophilic archaebacterium Halobacterium marismortui is presented. This has been achieved by the sequence analysis of peptides derived by enzymatic digestions with trypsin, pepsin and Staphylococcus aureus protease, as well as by chemical cleavage with cyanogen bromide and o-iodosobenzoic acid. The protein consists of 155 amino acid residues and has a molecular mass of 17545 Da. Comparison of this sequence with other ribosomal proteins by the computer programmes RELATE and ALIGN showed that the C-terminal two-thirds of H-S11 is homologous to the eubacterial ribosomal protein S15 and that the N-terminal one-third of H-S11 is possibly related to the N-terminal region of the eubacterial ribosomal protein S8. To explain this finding, possible genetic events during evolution, e.g. fusion or splitting of genes, are discussed.

UR - http://www.scopus.com/inward/record.url?scp=0022588158&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0022588158&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(86)80090-4

DO - 10.1016/0014-5793(86)80090-4

M3 - Article

AN - SCOPUS:0022588158

VL - 194

SP - 227

EP - 234

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 2

ER -