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Originally published In Press as doi:10.1074/jbc.M001041200 on July 25, 2000

J. Biol. Chem., Vol. 275, Issue 42, 33068-33076, October 20, 2000
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Chitin Catabolism in the Marine Bacterium Vibrio furnissii
IDENTIFICATION AND MOLECULAR CLONING OF A CHITOPORIN*

Nemat O. KeyhaniDagger , Xi-Bing Li, and Saul Roseman§

From the Department of Biology and the McCollum-Pratt Institute, The Johns Hopkins University, Baltimore, Maryland 21218

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 Roseman, S. (1996) J. Biol. Chem. 271, 33414-33424 and 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 molecular mass 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 Escherichia 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 nonmetabolizable analogue of (GlcNAc)2 at a reduced rate. These results imply that ChiP is a specific chitoporin.

* This work was supported by Grant GM51215 from the National Institutes of Health.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF129934.

Dagger Present address: Dept. of Microbiology and Cell Science, University of Florida, Gainesville, FL 32611.

§ To whom correspondence should be addressed: Dept. of Biology and the McCollum-Pratt Inst., Johns Hopkins University, Mudd Hall, Rm. 214, 3400 N. Charles St., Baltimore, MD 21218.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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