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

FEBS Letters

Hatakeyama, Tomomitsu¹  Kimura, Makoto¹  Hatakeyama, Tamiko¹ 

[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;    (H. marismortut);   

DOI  :  10.1016/0014-5793(88)80333-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown