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PMID: 2591382 Published · ppublish English Comparative Study Journal Article

Primary structures of five ribosomal proteins from the archaebacterium Halobacterium marismortui and their structural relationships to eubacterial and eukaryotic ribosomal proteins.

European journal of biochemistry ·Vol. 185 ·No. 3 ·1989-11-20 ·Pages 685-93

Hatakeyama T, Kaufmann F, Schroeter B, Hatakeyama T

Abstract

The complete amino acid sequences of ribosomal proteins L9, L20, L21/22, L24 and L32 from the archaebacterium Halobacterium marismortui were determined. The comparison of the sequences of these proteins with those from other organisms revealed that proteins L21/22 and L24 are homologous to ribosomal protein Yrp29 from yeast and L19 from rat, respectively, and that H. marismortui L20 is homologous to L30 from eubacteria. H. marismortui ribosomal protein L9 showed sequence homology to both L29 from yeast and L15 from eubacteria. No homologous protein was found for H. marismortui L32. These results are discussed with respect to the phylogenetic relationship between eubacteria, archaebacteria and eukaryotes.

MeSH Terms
Amino Acid Sequence Animals Bacterial Proteins Biological Evolution Eubacterium/chemistry Genes, Bacterial Halobacterium/chemistry,genetics Molecular Sequence Data RNA-Binding Proteins Rats Ribosomal Proteins/analysis Sequence Homology, Nucleic Acid Software Structure-Activity Relationship Yeasts/chemistry
Chemicals
Bacterial Proteins L20 ribosomal protein, bacteria RNA-Binding Proteins Ribosomal Proteins Rpl22 protein, rat ribosomal protein L24 ribosomal protein L32 ribosomal protein L21
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Hatakeyama T
Max-Planck-Institut für Molekulare Genetik, Abteilung Wittmann, Berlin.
Kaufmann F
Schroeter B
Hatakeyama T
Article Info
Journal
European journal of biochemistry
Abbr.
Eur J Biochem
ISSN
0014-2956
Published
1989-11-20
Pages
685-93
Language
English
Region
England
NLM ID
0107600
Subset
IM
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