UBIQUITIN FOUND IN THE ARCHAEBACTERIUM THERMOPLASMA-ACIDOPHILUM

被引：41

作者：

WOLF, S ^{[1
]}

LOTTSPEICH, F ^{[1
]}

BAUMEISTER, W ^{[1
]}

机构：

[1] MAX PLANCK INST BIOCHEM,KLOPFERSPITZ 18A,W-8033 MARTINSRIED,GERMANY

来源：

FEBS LETTERS | 1993年 / 326卷 / 1-3期

关键词：

UBIQUITIN; ARCHAEBACTERIUM (THERMOPLASMA-ACIDOPHILUM); 2-DIMENSIONAL ELECTROPHORESIS; MICROSEQUENCING;

D O I：

10.1016/0014-5793(93)81757-Q

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：

Systematic N-terminal sequencing of the low molecular weight proteins from Thermoplasma acidophilum separated by two-dimensional polyacrylamide gel electrophoresis led to the discovery of a polypeptide with an apparent M(r) of 4.5 kDa identical as its first 18 amino acid residues to human ubiquitin. The occurrence of ubiquitin and proteasomes in an archaebacterium strongly suggests that ATP-ubiquitin-dependent proteolysis is a cellular function that developed early in evolution.

引用

页码：42 / 44

页数：3

共 23 条

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