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Journal of Bacteriology, January 2001, p. 654-663, Vol. 183, No. 2
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.2.654-663.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

YkdA and YvtA, HtrA-Like Serine Proteases in Bacillus subtilis, Engage in Negative Autoregulation and Reciprocal Cross-Regulation of ykdA and yvtA Gene Expression

David Noone,^1,2 Alistair Howell,¹ Ross Collery,¹ and Kevin M. Devine^1,*

Department of Genetics, Smurfit Institute,¹ and National Pharmaceutical Biotechnology Centre,² Trinity College, Dublin 2, Ireland

Received 2 August 2000/Accepted 9 October 2000

HtrA-type serine proteases participate in folding and degradation of aberrant proteins and in processing and maturation of native proteins. Mutation of the corresponding genes often confers a pleiotropic phenotype that can include temperature sensitivity, sensitivity to osmotic and oxidative stress, and attenuated virulence. There are three HtrA-type serine proteases, YkdA, YvtA, and YycK, encoded in the Bacillus subtilis genome. In this report we show that YkdA and YvtA display many similarities: their expression profiles during the growth cycle in wild-type and mutant backgrounds are very alike, with expression being directed by very similar promoters. Both are induced by temperature upshift and by heterologous amylases at the transition phase of the growth cycle. These characteristics are quite different for YycK, suggesting that it has a cellular function distinct from that of the other two proteases or that it performs the same function but under different conditions. We also show that inactivation of either ykdA or yvtA results in compensating overexpression of the other gene, especially during stress conditions, with a concomitant increase in resistance to heat and hydrogen peroxide stresses. Mutation of both ykdA and yvtA leads to growth defects and to thermosensitivity. The fact that their expression increases dramatically at the transition phase of the growth cycle under certain conditions suggests that the YkdA and YvtA proteases may function in the processing, maturation, or secretion of extracellular enzymes in B. subtilis.

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^* Corresponding author. Mailing address: Department of Genetics, Smurfit Institute, Trinity College, Dublin 2, Ireland. Phone: (353)-1-6081872. Fax: (353)-1-6798558. E-mail: kdevine{at}tcd.ie.

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Journal of Bacteriology, January 2001, p. 654-663, Vol. 183, No. 2
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.2.654-663.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

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