Phosphate starvation affects the synthesis of outer membrane proteins in Thiobacillus ferrooxidans.
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.
Jerez
C A
CA
Departamento de Bioquímica, Facultad de Medicina, Universidad de Chile, Santiago.
Seeger
M
M
Amaro
A M
AM
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D015180:Electrophoresis, Gel, Two-Dimensional; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010710:Phosphates / Q000494:pharmacology*; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity; D013855:Thiobacillus / Q000187:drug effects* / Q000235:genetics / Q000378:metabolism
D001425:Bacterial Outer Membrane Proteins; D010710:Phosphates