AMINO-ACID-SEQUENCE OF THE RIBOSOMAL-PROTEIN HS23 FROM THE HALOPHILIC HALOARCULA-MARISMORTUI AND HOMOLOGY STUDIES TO OTHER RIBOSOMAL-PROTEINS

被引：3

作者：

ENGEMANN, S ^{[1
]}

HERFURTH, E ^{[1
]}

BRIESEMEISTER, U ^{[1
]}

WITTMANNLIEBOLD, B ^{[1
]}

机构：

[1] MAX DELBRUCK CENTRUM MOLEK MED,PROT CHEM ABT,D-13125 BERLIN,GERMANY

来源：

JOURNAL OF PROTEIN CHEMISTRY | 1995年 / 14卷 / 04期

关键词：

RIBOSOMAL PROTEINS; PROTEIN SEQUENCING; EVOLUTION; HALOARCULA MARISMORTUI;

D O I：

10.1007/BF01886759

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 ribosomal protein HS23 from the 30S subunit of the extreme halophilic Haloarcula marismortui, belonging to the group of archaea, was isolated either by RP-HLPLC or two-dimensional polyacrylamide gel electrophoresis. The complete amino acid sequence was determined by automated N-terminal microsequencing. The protein consists of 123 residues with a corresponding molecular mass of 12,552 Da as determined by electrospray mass spectroscopy; the pI is 11.04. Homology studies reveal similarities to the eukaryotic ribosomal protein S8 from Home sapiens, Rattus norvegicus, Leishmania major, and Saccharomyces cerevisiae.

引用

页码：189 / 195

页数：7

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