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Journal of Bacteriology, December 2001, p. 7044-7052, Vol. 183, No. 24
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.24.7044-7052.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Characterization of Pseudomonas aeruginosa Chitinase, a Gradually Secreted Protein

Jindra Folders,1,dagger Jon Algra,1 Marc S. Roelofs,1 Leendert C. van Loon,2 Jan Tommassen,1,* and Wilbert Bitter1,3

Department of Molecular Microbiology, Institute of Biomembranes,1 and Department of Plant Pathology,2 Utrecht University, Utrecht, and Department of Medical Microbiology, Vrije Universiteit, Amsterdam,3 The Netherlands

Received 6 April 2001/Accepted 18 September 2001

The gram-negative bacterium Pseudomonas aeruginosa secretes many proteins into its extracellular environment via the type I, II, and III secretion systems. In this study, a gene, chiC, coding for an extracellular chitinolytic enzyme, was identified. The chiC gene encodes a polypeptide of 483 amino acid residues, without a typical N-terminal signal sequence. Nevertheless, an N-terminal segment of 11 residues was found to be cleaved off in the secreted protein. The protein shows sequence similarity to the secreted chitinases ChiC of Serratia marcescens, ChiA of Vibrio harveyi, and ChiD of Bacillus circulans and consists of an activity domain and a chitin-binding domain, which are separated by a fibronectin type III domain. ChiC was able to bind and degrade colloidal chitin and was active on the artificial substrates carboxymethyl-chitin-Remazol Brilliant Violet and p-nitrophenyl-beta -D-N,N',N"-triacetylchitotriose, but not on p-nitrophenyl-beta -D-N-acetylglucosamine, indicating that it is an endochitinase. Expression of the chiC gene appears to be regulated by the quorum-sensing system of P. aeruginosa, since this gene was not expressed in a lasIR vsmI mutant. After overnight growth, the majority of the ChiC produced was found intracellularly, whereas only small amounts were detected in the culture medium. However, after several days, the cellular pool of ChiC was largely depleted, and the protein was found in the culture medium. This release could not be ascribed to cell lysis. Since ChiC did not appear to be secreted via any of the known secretion systems, a novel secretion pathway seems to be involved.

* Corresponding author. Mailing address: Department of Molecular Microbiology, Padualaan 8, 3584 CH Utrecht, The Netherlands. Phone: (31) 30 253 2999. Fax: (31) 30 251 3655. E-mail: J.P.M.Tommassen{at}bio.uu.nl.

dagger Present address: Plant Research International, 6700 AA Wageningen, The Netherlands.

Journal of Bacteriology, December 2001, p. 7044-7052, Vol. 183, No. 24
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.24.7044-7052.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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