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Journal of Bacteriology, May 2002, p. 2780-2788, Vol. 184, No. 10
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.10.2780-2788.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

The E1ß and E2 Subunits of the Bacillus subtilis Pyruvate Dehydrogenase Complex Are Involved in Regulation of Sporulation

Haichun Gao,1 Xin Jiang,2 Kit Pogliano,2 and Arthur I. Aronson1*

Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907,1 Division of Biology, University of California at San Diego, La Jolla, California 92093-03492

Received 12 November 2001/ Accepted 19 February 2002

The pdhABCD operon of Bacillus subtilis encodes the pyruvate decarboxylase (E1{alpha} and E1ß), dihydrolipoamide acetyltransferase (E2), and dihydrolipoamide dehydrogenase (E3) subunits of the pyruvate dehydrogenase multienzyme complex (PDH). There are two promoters: one for the entire operon and an internal one in front of the pdhC gene. The latter may serve to ensure adequate quantities of the E2 and E3 subunits, which are needed in greater amounts than E1{alpha} and E1ß. Disruptions of the pdhB, pdhC, and pdhD genes were isolated, but attempts to construct a pdhA mutant were unsuccessful, suggesting that E1{alpha} is essential. The three mutants lacked PDH activity, were unable to grow on glucose and grew poorly in an enriched medium. The pdhB and pdhC mutants sporulated to only 5% of the wild-type level, whereas the pdhD mutant strain sporulated to 55% of the wild-type level. This difference indicated that the sporulation defect of the pdhB and pdhC mutant strains was due to a function(s) of these subunits independent of enzymatic activity. Growth, but not low sporulation, was enhanced by the addition of acetate, glutamate, succinate, and divalent cations. Results from the expression of various spo-lacZ fusions revealed that the pdhB mutant was defective in the late stages of engulfment or membrane fusion (stage II), whereas the pdhC mutant was blocked after the completion of engulfment (stage III). This analysis was confirmed by fluorescent membrane staining. The E1ß and E2 subunits which are present in the soluble fraction of sporulating cells appear to function independently of enzymatic activity as checkpoints for stage II-III of sporulation.

* Corresponding author. Mailing address: Department of Biological Sciences, Purdue University, West Lafayette, IN 47907. Phone: (765) 494-4992. Fax: (765) 494-0876. E-mail: aaronson{at}bilbo.bio.purdue.edu.

Journal of Bacteriology, May 2002, p. 2780-2788, Vol. 184, No. 10
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.10.2780-2788.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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