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Microbiology & Fermentation Technology

Regulation of the chitin degradation and utilization system by the ChiX small RNA in Serratia marcescens 2170

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Pages 376-385 | Received 05 Jun 2015, Accepted 30 Jul 2015, Published online: 12 Sep 2015
 

Abstract

Serratia marcescens 2170 produces three different types of chitinases and chitin-binding protein CBP21. We found that transposon insertion into the 5′ untranslated region (5′ UTR) of chiPQ-ctb led to defective chitinase and CBP21 production. ChiX small RNA possessed the complementary sequence of the 5′ UTRs of the chiPQ-ctb and chiR and repressed the expression of chiP and chiR. ChiX was detected in a medium containing glucose, glycerol, GlcNAc, and (GlcNAc)2, but the expression of both chiP and chiR was only observed in a medium containing (GlcNAc)2. ∆chiX mutant produced chitinases, CBP21, and chitobiase without induction. chiP transcripts were more abundant than those of chiR or chiX in a medium containing (GlcNAc)2. These results suggest that the constitutively expressed ChiX binds to the highly abundant chiP 5′ UTR, thereby leading to the induction of chiR mRNA translation and the subsequent expression of chitinases and CBP21.

Graphical abstract

Small RNA, ChiX, coordinates the synchronized expression of chitin-degrading enzymes and the system for incorporating chitin degradation products in Serratia marcescens.

Acknowledgments

We thank Prof. Kazuhide Totani, National Institute of Technology, Ichinoseki College, for providing N,N′-diacetylchitobiose, Yaizu Suisankagaku Industry for N,N′-diacetylchitobiose and water-soluble chitin.

Disclosure statement

No potential conflict of interest was reported by the authors.

Notes

Abbreviations: GlcNAc, N-acetylglucosamine; (GlcNAc)2, N,N′-diacetylchitobiose; 5 UTR, 5 untranslated region; RT-PCR, reverse transcription polymerase chain reaction; RACE, rapid amplification of cDNA ends; sRNA, small RNA; IGR, intergenic region; YEM medium, yeast extract-supplemented minimal medium; CBM, carbohydrate binding module; PTS, phosphoenolpyruvate-dependent sugar phosphotransferase system.

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