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A more recent version of this article appeared on October 13, 2000
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M001041200v1
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Papers In Press, published online ahead of print July 25, 2000
J. Biol. Chem, 10.1074/jbc.M001041200
Submitted on February 8, 2000
Revised on May 25, 2000
Accepted on July 25, 2000

Chitin Catabolism in the Marine Bacterium Vibrio furnissii: Identification and Molecular Cloning of a Chitoporin

Nemat O. Keyhani, Xi-Bing Li, and Saul Roseman

Department of Biology, Johns Hopkins University, Baltimore, MD 21218

Corresponding Author: roseman{at}jhu.edu

Chitin catabolism by the marine bacterium Vibrio furnissii involves many genes and proteins, including two unique periplasmic hydrolases, a chitodextrinase and a beta -N-acetylglucosaminidase (Keyhani, N.O. and S. Roseman. (1996) J. Biol. Chem. 271: 33414-33424; 33425-33432). A specific chitoporin in the outer membrane may be required for these glycosidases to be accessible to extracellular chitooligosaccharides, (GlcNAc)n, that are produced by chitinases. We report here the identification and molecular cloning of such a porin. An outer membrane protein, OMP, (apparent Mr, 40 kDa) was expressed when V. furnissii was induced by (GlcNAc) n, n = 2-6, but not by GlcNAc or other sugars. Based on the N-terminal sequence of OMP, oligonucleotides were synthesized and used to clone the gene, chiP. The deduced amino acid sequence of ChiP is similar to several bacterial porins; OMP is a processed form of ChiP. In Escherichai coli, two recombinant proteins were observed, corresponding to processed and unprocessed forms of ChiP. A null mutant of chiP was constructed in V. furnissii. In contrast to the parental strain, the mutant did not grow on (GlcNAc)3, and transported a non-metabolizable analogue of (GlcNAc)2 at a reduced rate. These results imply that ChiP is a specific chitoporin.


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