Post-translational control of the Streptomyces lividans ClgR regulon by ClpP

• Published in: Microbiology (Society for General Microbiology) 2006-04, Vol.152 (4), p.1021-1027
• Main Authors: Bellier, Audrey, Gominet, Myriam, Mazodier, Philippe
• Format: Article
• Language: English
• Subjects: Bacterial Proteins; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Blotting, Western; Endopeptidase Clp; Endopeptidase Clp - metabolism; Gene Expression Regulation, Bacterial; Life Sciences; Operon; Other; Protease La; Protease La - metabolism; Regulon; Reverse Transcriptase Polymerase Chain Reaction; RNA, Bacterial; RNA, Bacterial - analysis; RNA, Messenger; RNA, Messenger - analysis; Streptomyces lividans; Streptomyces lividans - enzymology; Streptomyces lividans - genetics; Trans-Activators; Trans-Activators - genetics; Trans-Activators - metabolism; Transcription, Genetic
• ISSN: 1350-0872; 1465-2080
• DOI: 10.1099/mic.0.28564-0

Unité Postulante de Génétique Bactérienne et Différenciation, CNRS URA 2172, Institut Pasteur, 25 rue Dr Roux, 75724 Paris Cedex 15, France Correspondence Philippe Mazodier mazodier{at}pasteur.fr It has been shown previously that expression of the Streptomyces lividans clpP1P2 operon, encoding proteolytic subunits of the Clp complex, the clpC1 gene, encoding the ATPase subunit, and the lon gene, encoding another ATP-dependent protease, are all activated by ClgR. The ClgR regulon also includes the clgR gene itself. It is shown here that the degradation of ClgR and Lon is ClpP1/P2-dependent and that the two C-terminal alanines of these new substrates are involved in their stability. The ClpC1 protein, which does not end with two alanines, is also accumulated in a clpP1P2 mutant. The results presented here support the idea that ClpP1/P2 ensure post-translational control of ClgR regulon members, including ClgR itself.