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Research Paper |
Unité de Biochimie Microbienne, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris Cedex 15, France1
VIVALIS SA, CHU de Nantes Hôtel-Dieu, Place A. Ricordeau, 44093 Nantes Cedex 1, France2
Author for correspondence: Philippe Mazodier. Tel: +33 1 45 68 88 42. Fax: +33 1 45 68 89 38. e-mail: mazodier{at}pasteur.fr
Members of a family of ATP-dependent proteases related to Lon from Escherichia coli are present in most prokaryotes and eukaryotes. These proteases are generally reported to be heat induced, and various regulatory systems have been described. The authors cloned and disrupted the lon gene and studied the regulation of its expression in Streptomyces lividans. lon is negatively regulated by the HspR/HAIR repressor/operator system, suggesting that Lon is produced concomitantly with the other members of this regulon, DnaK and ClpB. The lon mutant grew more slowly than the wild-type and spore germination was impaired at high temperature. Nevertheless its cell cycle was not greatly affected and it sporulated normally.
Keywords: heat shock regulation, Streptomyces, HspR, protease, DnaK
Abbreviations: HSP, heat-shock protein
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