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Characterization and environmental regulation of outer membrane proteins in Xenorhabdus nematophilus. Appl Environ Microbiol 1995 Jan;61(1):200-4

Date

01/01/1995

Pubmed ID

7887602

Pubmed Central ID

PMC167275

DOI

10.1128/AEM.61.1.200-204.1995

Abstract

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 SA

Author

Steven Forst PhD Professor in the Biological Sciences department at University of Wisconsin - Milwaukee




MESH terms used to index this publication - Major topics in bold

Amino Acid Sequence
Bacterial Outer Membrane Proteins
Enterobacteriaceae
Escherichia coli
Molecular Sequence Data
Sequence Alignment
Temperature
jenkins-FCD Prod-482 91ad8a360b6da540234915ea01ff80e38bfdb40a