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An outer membrane protein (OmpA) of Escherichia coli can be translocated across the cytoplasmic membrane of Bacillus subtllis
Author(s) -
Meens Jochen,
Frings EIke,
Klose Michael,
Freudl Roland
Publication year - 1993
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1993.tb01743.x
Subject(s) - biology , bacillus subtilis , signal peptide , escherichia coli , bacterial outer membrane , signal peptidase , secretory protein , biochemistry , cytoplasm , proteases , vesicle associated membrane protein 8 , membrane protein , bacteria , peptide sequence , microbiology and biotechnology , secretion , membrane , gene , genetics , enzyme
Summary The translocation of secretory proteins derived from a Gram‐positive (Staphylococcus hyicus prolipase) or a Gram‐negative (Escherichia coli pre‐OmpA protein) bacterium across the cytoplasmic membrane was studied in E. coli and Bacillus subtilis. in both microorganisms, the prolipase was found to be secreted across the plasma membrane when either the pre‐prolipase signal peptide (38 amino acids in length) or the pre‐OmpA signal peptide (21 amino acids in length) was used. Expression of the gene encoding the authentic pre‐OmpA protein in B. subtilis resulted in the translocation of mature OmpA protein across the plasma membrane. Processing of the OmpA precursor in B. subtilis required the electrochemical potential and was sensitive to sodium azide, suggesting that the B. subtilis SecA homologue was involved in the translocation process. The mature OmpA protein, which was most likely present in an aggregated state, was fully accessible to proteases in protoplasted cells. Therefore, our results clearly demonstrate that an outer membrane protein can be secreted by B. subtilis , supporting the notion that the basic mechanism of protein translocation is highly conserved in Gram‐positive and Gram‐negative bacteria.