Open AccessFunctional complementation of E. coli secD and secG mutants by Helicobacter pylori homologues
Author(s) -
Fitchen Nicola,
Williams Paul,
Hardie Kim R.
Publication year - 2003
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 - 10.1016/s0378-1097(03)00786-9
Subject(s) - complementation , helicobacter pylori , protein fragment complementation assay , mutant , secretion , biology , cytoplasm , bacterial outer membrane , escherichia coli , microbiology and biotechnology , membrane protein , biochemistry , genetics , gene , membrane
The Sec machinery is one mechanism used by bacteria to translocate proteins across their cytoplasmic membrane. Most of the Sec components have been identified within the important gastric pathogen, Helicobacter pylori , however their functionality has not yet been demonstrated. Here we report the existence of putative homologues to the Sec components yajC (HP1450) and yidC (HP1551), and demonstrate the ability of the H. pylori secD (HP1550) and secG (HP1255) homologues to facilitate inner membrane translocation of the maltose‐binding protein MalE, by complementation of the respective secretion‐deficient Escherichia coli mutants, thus providing evidence of their functionality.