
Phosphate starvation affects the synthesis of outer membrane proteins in Thiobacillus ferrooxidans
Author(s) -
Jerez Carlos A.,
Seeger Michael,
Amaro Ana M.
Publication year - 1992
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.1574-6968.1992.tb05485.x
Subject(s) - bacterial outer membrane , porin , pseudomonas stutzeri , outer membrane efflux proteins , biochemistry , escherichia coli , enterobacter cloacae , biology , peptide sequence , amino acid , microbiology and biotechnology , periplasmic space , enterobacteriaceae , inner membrane , chemistry , bacteria , membrane , genetics , gene
The outer membrane protein (omp40) component from the chemolithoautotrophic acidophilic Thiobacillus ferrooxidans is apparently regulated by the external pH and the concentration of phosphorus. Its amino‐terminal sequence showed little identity with the Escherichia coli OmpC, OmpF or PhoE porins, but was 38.5% identical to the outer membrane channel‐forming protein NosA from Pseudomonas stutzeri , whose expression is also regulated environmentally. In addition, the partial amino acid sequence of T. ferrooxidans omp40 showed between 34 and 38% identity with the amino‐terminal end of the small outer membrane proteins Rck and PagC from Salmonella typhimurium and OmpX from Enterobacter cloacae .