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Journal of Bacteriology, September 2002, p. 5141-5150, Vol. 184, No. 18
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.18.5141-5150.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Characterization of bcsA Mutations That Bypass Two Distinct Signaling Requirements for Myxococcus xanthus Development

John K. Cusick,,{dagger} Elizabeth Hager, and Ronald E. Gill*

Department of Microbiology, University of Colorado Health Sciences Center, Denver, Colorado 80262

Received 3 December 2001/ Accepted 18 June 2002

The BsgA protease is required for starvation-induced development in Myxococcus xanthus. Bypass suppressors of a bsgA mutant were isolated to identify genes that may encode additional components of BsgA protease-dependent regulation of development. Strain M951 was isolated following Tn5 mutagenesis of a bsgA mutant and was capable of forming fruiting bodies and viable spores in the absence of the BsgA protease. The Tn5{Omega}951 insertion was localized to a gene, bcsA, that encodes a protein that has significant amino acid similarity to a group of recently described flavin-containing monooxygenases involved in styrene catabolism. Mutations in bcsA bypassed the developmental requirements for both extracellular B and C signaling but did not bypass the requirement for A signaling. Bypass of the B-signaling requirement by the bcsA mutation was accompanied by restored expression of a subset of developmentally induced lacZ fusions to the BsgA protease-deficient strain. bcsA mutant cells developed considerably faster than wild-type cells at low cell density and altered transcriptional levels of a developmentally induced, cell-density-regulated gene ({Omega}4427), suggesting that the bcsA gene product may normally act to inhibit development in a cell-density-regulated fashion. Bypass of the requirements for both B and C signaling by bcsA mutations suggests a possible link between these two genetically, biochemically, and temporally distinct signaling requirements.

* Corresponding author. Mailing address: Department of Microbiology, University of Colorado Health Sciences Center, 4200 East Ninth Ave., B175, Denver, CO 80262. Phone: (303) 315-7832. Fax: (303) 315-6785. E-mail: ron.gill{at}UCHSC.edu.

{dagger} Present address: Department of Immunology, National Jewish Medical and Research Center, Denver, CO 80206.

Journal of Bacteriology, September 2002, p. 5141-5150, Vol. 184, No. 18
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.18.5141-5150.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Rasmussen, A. A., Sogaard-Andersen, L. (2003). TodK, a Putative Histidine Protein Kinase, Regulates Timing of Fruiting Body Morphogenesis in Myxococcus xanthus. J. Bacteriol. 185: 5452-5464 [Abstract] [Full Text]  


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