A PROTEIN WITH SEQUENCE IDENTITY TO SKP (FIRA) SUPPORTS PROTEIN TRANSLOCATION INTO PLASMA-MEMBRANE VESICLES OF ESCHERICHIA-COLI

被引：29
|
作者：
THOME, BM
HOFFSCHULTE, HK
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 | 1990年 / 269卷 / 01期
关键词：
Export factor; FirA; Inside-out plasma membrane vesicle; Protein export; SecA; Skp;
D O I：
10.1016/0014-5793(90)81132-8
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：
We have purified to homogeneity a 15 kDa-protein from a ribosomal salt extract of Escherichia coli that compensates in vitro a defect of SecA but not of SecB. Removal of this protein from a cell-free transcription/translation system impairs translocation into plasma membrane vesicles of the precursors of LamB and to a lesser degree also of OmpA. These results suggest a role of the 15 kDa-protein in bacterial protein export. The NH2-terminal 35 amino acids were found to be identical to those of the skp (firA) gene product, to which several putative functions have previously been attributed. © 1990.
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页码：113 / 116
页数：4
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