The ATPase ClpX is conditionally involved in the morphological differentiation of Streptomyces lividans

ATP-dependent proteases of the ClpP type are widespread in eubacteria. These proteolytic complexes are composed of a proteolytic subunit and an ATPase subunit. They are involved in the degradation of denatured proteins, but also play a role in specific regulatory pathways. In Streptomyces lividans s...

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Veröffentlicht in:Molecular genetics and genomics : MGG 2003-02, Vol.268 (5), p.563-569
Hauptverfasser: Viala, J, Mazodier, P
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description ATP-dependent proteases of the ClpP type are widespread in eubacteria. These proteolytic complexes are composed of a proteolytic subunit and an ATPase subunit. They are involved in the degradation of denatured proteins, but also play a role in specific regulatory pathways. In Streptomyces lividans strains which lack the proteolytic subunit ClpP1, cell cycle progression has been shown to be blocked at early stages of growth. In this study, we examined the role of the ATPase subunit ClpX, a possible partner of the products of the clpP1 operon. A clpX mutant was obtained and it was shown that its growth was impaired only on acidic medium. Thus, the clpX phenotype differs from the clpP1 phenotype, indicating that these two components have only partially overlapping roles. We also analyzed the expression of clpX. Although clpX expression is increased under heat-shock conditions in many bacteria, we found that this is not the case in S. lividans.
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These proteolytic complexes are composed of a proteolytic subunit and an ATPase subunit. They are involved in the degradation of denatured proteins, but also play a role in specific regulatory pathways. In Streptomyces lividans strains which lack the proteolytic subunit ClpP1, cell cycle progression has been shown to be blocked at early stages of growth. In this study, we examined the role of the ATPase subunit ClpX, a possible partner of the products of the clpP1 operon. A clpX mutant was obtained and it was shown that its growth was impaired only on acidic medium. Thus, the clpX phenotype differs from the clpP1 phenotype, indicating that these two components have only partially overlapping roles. We also analyzed the expression of clpX. 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subjects Adenosine Triphosphatases
Adenosine Triphosphatases - genetics
Adenosine Triphosphatases - metabolism
Amino Acid Sequence
Antibiotics
ATPases Associated with Diverse Cellular Activities
Bacteria
Bacterial Proteins
Base Sequence
Cell Cycle
E coli
Endopeptidase Clp
Escherichia coli Proteins
Gene Expression
Genes
Genes, Bacterial
Genetic Complementation Test
Genomes
Genomics
Genotype & phenotype
Hydrogen-Ion Concentration
Life Sciences
Molecular Chaperones
Molecular Sequence Data
Morphology
Mutation
Phenotype
Plasmids
Plasmids - genetics
Proteins
Serine Endopeptidases
Serine Endopeptidases - genetics
Serine Endopeptidases - metabolism
Streptomyces
Streptomyces - cytology
Streptomyces - enzymology
Streptomyces - genetics
title The ATPase ClpX is conditionally involved in the morphological differentiation of Streptomyces lividans
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