Open AccessIs the CvaA* protein, encoded within the colicin V export gene cvaA , required for colicin V transport?
Author(s) -
Skvirsky Rachel C,
Shen Xiaoyu,
Reginald Shoba
Publication year - 1996
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1996.tb08157.x
Subject(s) - colicin , signal peptide , escherichia coli , fusion protein , biology , gene , membrane protein , transport protein , bacterial outer membrane , coding region , bacteriocin , peptide sequence , nuclear export signal , genetics , bacteria , recombinant dna , rna , membrane
The antibacterial peptide toxin colicin V is exported from Escherichia coli cells by a signal sequence‐independent, ABC export system. Export requires at least three proteins ‐membrane fusion protein CvaA, ABC export protein CvaB, and outer membrane protein TolC. The cvaA gene also encodes a second protein, CvaA*, initiated from an in‐frame translational re‐start within the cvaA coding sequence. To determine whether the internally encoded CvaA* protein also functions in the export pathway, the putative start codons for CvaA* were mutagenized, while maintaining CvaA function. Elimination of CvaA* translation caused no change in colicin V export levels, indicating that the CvaA* protein is not required in the secretion pathway.