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PMID: 3191994 Published · ppublish English Comparative Study Journal Article

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

FEBS letters ·Vol. 240 ·No. 1-2 ·1988-11-21 ·Pages 21-8

Hatakeyama T, Hatakeyama T, Kimura M

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 13,538, 16,812 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.

MeSH Terms
Amino Acid Sequence Aniline Compounds Archaeal Proteins Biological Evolution Escherichia coli Proteins Halobacterium/genetics Molecular Sequence Data Ribosomal Proteins/genetics Solubility
Chemicals
Aniline Compounds Archaeal Proteins Escherichia coli Proteins Ribosomal Proteins ribosomal protein L16 ribosomal protein L23, E coli ribosomal protein L33, archaea rpmG protein, E coli 4-trifluoromethylaniline
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Hatakeyama T
Max-Planck-Institut für Molekulare Genetik, Abteilung Wittmann, Berlin, Germany.
Hatakeyama T
Kimura M
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1988-11-21
Pages
21-8
Language
English
Region
England
NLM ID
0155157
Subset
IM
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