IDENTIFICATION AND SOLUBILIZATION OF A SIGNAL PEPTIDASE FROM THE PHOTOTROPHIC BACTERIUM RHODOBACTER-CAPSULATUS

被引:14
作者
WIESELER, B
SCHILTZ, E
MULLER, M
机构
[1] UNIV FREIBURG, INST BIOCHEM, HERMANN HERDER STR 7, W-7800 FREIBURG, GERMANY
[2] UNIV FREIBURG, INST ORGAN CHEM & BIOCHEM, W-7800 FREIBURG, GERMANY
来源
FEBS LETTERS | 1992年 / 298卷 / 2-3期
关键词
SIGNAL PEPTIDASE; PROTEIN EXPORT; RHODOBACTER-CAPSULATUS; PHOTOTROPHIC BACTERIA;
D O I
10.1016/0014-5793(92)80075-R
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
In Gram-negative bacteria, exported proteins are synthesized with an amino-terminal signal sequence which is cleaved off by the signal peptidase during, or shortly after the translocation process. Here, we report the identification and solubilization of a signal peptidase from the phototrophic bacterium Rhodobacter capsulatus which cleaves homologous and heterologous precursor proteins at the authentic cleavage site. This signal peptidase is the first identified component of the R. capsulatus protein export machinery.
引用
收藏
页码:273 / 276
页数:4
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