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