Primary structures of three highly acidic ribosomal proteins S6, S12 and S15 from the archaebacterium Halobacterium marismortui

FEBS Letters

Kimura, Makoto¹  Arndt, Evelyn¹  Kimura, Junko¹ 

[1] Max-Planck-Institut für Molekulare Genetik, Abteilung Wittmann, D-1000 Berlin 33 (Dahlem), Germany

关键词: Amino acid sequence;    Ribosomal protein;    Sequence comparison;    (Halobacterium marismortui);   

DOI  :  10.1016/0014-5793(87)80423-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The amino acid sequences of three extremely acidic ribosomal proteins, S6, S12, and S15, from Halobacterium marismortui have been determined. The sequences were obtained by the sequence analysis of peptides derived by enzymatic digestion with trypsin. Stapylococcus aureus protease and chymotrypsin, as well as by cleavage with dilute HCl. The proteins, S6, S12 and S15, consist of 116, 147 and 102 amino acid residues, and have molecular masses of 12251, 16440 and 11747 Da, respectively. Comparison of the amino acid sequences of these proteins with ribosomal protein sequences of other organisms revealed that halobacterial protein S12 has homology with the eukaryotic protein S16A from Saccharomyces cerevisiae, while S15 is significantly related to the Xenopus laevis S19 protein. No homology was found between these halobacterial proteins and any eubacterial ribosomal proteins.

【 授权许可】

Unknown