A protein with sequence identity to Skp (FirA) supports protein translocation into plasma membrane vesicles of Escherichia coli

FEBS Letters

Schiltz, Emile²  Hoffschulte, Hedda K.¹  Müller, Matthias¹  Thome, Birgit M.¹ 

[1] The Institutes of Biochemistry, University of Freiburg, Hermann-Herder-Str. 7, D-7800 Freiburg, FRG;The Institutes of Organic Chemistry and Biochemistry, University of Freiburg, Hermann-Herder-Str. 7, D-7800 Freiburg, FRG

关键词: Protein export;    Skp;    FirA;    Inside-out plasma membrane vesicle;    SecA;    Export factor;    INV;    inverted plasma membrane vesicles;    K-INV;    salt-extracted INV;   

DOI  :  10.1016/0014-5793(90)81132-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown