The primary structures of ribosomal proteins L16, L23 and L33 from the archaebacterium Halobacterium marismortui

Tomomitsu Hatakeyama, Tamiko Hatakeyama, Makoto Kimura

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

The complete amino acid sequences of ribosomal proteins L16, L23 and L33 from the archaebacterium Halobacterium marismortui were determined. The sequences were established by manual sequencing of peptides produced with several proteases as well as by cleavage with dilute HCl. Proteins L16, L23 and L33 consist of 119, 154 and 69 amino acid residues, and their molecular masses are 13538, 16812 and 7620 Da, respectively. The comparison of their sequences with those of ribosomal proteins from other organisms revealed that L23 and L33 are related to eubacterial ribosomal proteins from Escherichia coli and Bacillus stearothermophilus, while protein L16 was found to be homologous to a eukaryotic ribosomal protein from yeast. These results provide information about the special phylogenetic position of archaebacteria.

Original languageEnglish
Pages (from-to)21-28
Number of pages8
JournalFEBS Letters
Volume240
Issue number1-2
DOIs
Publication statusPublished - Nov 21 1988

All Science Journal Classification (ASJC) codes

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

Fingerprint Dive into the research topics of 'The primary structures of ribosomal proteins L16, L23 and L33 from the archaebacterium Halobacterium marismortui'. Together they form a unique fingerprint.

  • Cite this