Characterization and environmental regulation of outer membrane proteins in Xenorhabdus nematophilus. Appl Environ Microbiol 1995 Jan;61(1):200-4
Date
01/01/1995Pubmed ID
7887602Pubmed Central ID
PMC167275DOI
10.1128/aem.61.1.200-204.1995Scopus ID
2-s2.0-0028847646 (requires institutional sign-in at Scopus site) 35 CitationsAbstract
We have examined the production of the outer membrane proteins of the primary and secondary forms of Xenorhabdus nematophilus during exponential- and stationary-phase growth at different temperatures. The most highly expressed outer membrane protein of X. nematophilus was OpnP. The amino acid composition of OpnP was very similar to those of the porin proteins OmpF and OmpC of Escherichia coli. N-terminal amino acid sequence analysis revealed that residues 1 to 27 of the mature OpnP shared 70 and 60% sequence identities with OmpC and OmpF, respectively. These results suggest that OpnP is a major porin protein in X. nematophilus. Three additional proteins, OpnA, OpnB, and OpnS, were induced during stationary-phase growth. OpnB was present at a high level in stationary-phase cells grown at 19 to 30 degrees C and was repressed in cells grown at 34 degrees C. OpnA was optimally produced at 30 degrees C and was not present in cells grown at lower and higher temperatures. The production of OpnS was not dependent on growth temperature. In contrast, another outer membrane protein, OpnT, was strongly induced as the growth temperature was elevated from 19 to 34 degrees C. In addition, we show that the stationary-phase proteins OpnA and OpnB were not produced in secondary-form cells.
Author List
Leisman GB, Waukau J, Forst SAAuthor
Steven Forst PhD Professor in the Biological Sciences department at University of Wisconsin - MilwaukeeMESH terms used to index this publication - Major topics in bold
Amino Acid SequenceBacterial Outer Membrane Proteins
Enterobacteriaceae
Escherichia coli
Molecular Sequence Data
Sequence Alignment
Temperature
