AMINO-ACID-SEQUENCES OF THE RIBOSOMAL-PROTEINS HL30 AND HMAL5 FROM THE ARCHAEBACTERIUM HALOBACTERIUM-MARISMORTUI

被引：14

作者：

HATAKEYAMA, T ^{[1
]}

机构：

[1] MAX PLANCK INST MOLEC GENET,ABT WITTMAN,W-1000 BERLIN 33,GERMANY

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1990年 / 1039卷 / 03期

关键词：

(H. marismortu); Acetylation; amino terminal; Amino acid sequence; Amino terminal acetylation; Archaebacterium; Evolution; Ribosomal protein;

D O I：

10.1016/0167-4838(90)90269-L

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The complete amino acid sequences of the ribosomal proteins HL30 and HmaL5 from the archaebacteruim Halobacterium marismortui were determined. Protein HL30 was found to be acetylated at its N-terminal amino acid and shows homology to the eukaryotic ribosomal proteins YL34 from yeast and RL31 from rat. Protein HmaL5 was homologous to the protein L5 from Escherichia coli and Bacillus stearothermophilus as well as to YL16 from yeast. HmaL5 shows more similarities to its eukaryotic counterpart than to eubacterial ones. © 1990.

引用

页码：343 / 347

页数：5

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