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Microbiology 155 (2009), 3652-3660; DOI  10.1099/mic.0.029496-0
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Microbiology 155 (2009), 3652-3660; DOI  10.1099/mic.0.029496-0
© 2009 Society for General Microbiology

Identification of a second β-glucoside phosphoenolpyruvate : carbohydrate phosphotransferase system in Corynebacterium glutamicum R

Yuya Tanaka, Haruhiko Teramoto, Masayuki Inui and Hideaki Yukawa

Research Institute of Innovative Technology for the Earth, 9-2, Kizugawadai, Kizugawa, Kyoto 619-0292, Japan

The phosphoenolpyruvate : carbohydrate phosphotransferase system (PTS) catalyses carbohydrate transport by coupling it to phosphorylation. Previously, we reported a Corynebacterium glutamicum R β-glucoside PTS encoded by bglF. Here we report that C. glutamicum R contains an additional β-glucoside PTS gene, bglF2, organized in a cluster with a putative phospho-β-glucosidase gene, bglA2, and a putative antiterminator, bglG2. While single gene disruption strains of either bglF or bglF2 were able to utilize salicin or arbutin as sole carbon sources, a double disruption strain exhibited defects in utilization of both carbon sources. Expression of both bglF and bglF2 was induced in the presence of either salicin or arbutin, although disruption of bglG2 affected only bglF2 expression. Moreover, in the presence of either salicin or arbutin, glucose completely repressed the expression of bglF but only slightly repressed that of bglF2. We conclude that BglF and BglF2 have a redundant role in β-glucoside transport even though the catabolite repression control of their encoding genes is different. We also show that expression of both bglF and bglF2 requires the general PTS.

Correspondence
Hideaki Yukawa
mmg-lab{at}rite.or.jp


Abbreviations: PRD, PTS regulation domain; PTS, phosphoenolpyruvate : carbohydrate phosphotransferase system; RAT, ribonucleic antiterminator

A supplementary table of primers is available with the online version of this paper.







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