FEBS Lett. 1990 Aug 20;269(1):113-6.

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

Thome BM, Hoffschulte HK, Schiltz E, Müller M.

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Institute of Biochemistry, University of Freiburg, FRG.

Abstract

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.

PMID:: 2167239; [PubMed - indexed for MEDLINE]

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Research Support, Non-U.S. Gov't

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Bacterial Proteins

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Precursor-specific requirements for SecA, SecB, and delta muH+ during protein export of Escherichia coli. [J Biol Chem. 1994]
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