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 |
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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. Although clpX expression is increased under heat-shock conditions in many bacteria, we found that this is not the case in S. lividans.</description><identifier>ISSN: 1617-4615</identifier><identifier>EISSN: 1617-4623</identifier><identifier>DOI: 10.1007/s00438-002-0783-1</identifier><identifier>PMID: 12589431</identifier><language>eng</language><publisher>Germany: Springer Nature B.V</publisher><subject>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</subject><ispartof>Molecular genetics and genomics : MGG, 2003-02, Vol.268 (5), p.563-569</ispartof><rights>Springer-Verlag 2003</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c389t-7a49096f04d8a3ce48f5b6df54e8705f58320876af2c40aaab36ab3128244f6f3</citedby><cites>FETCH-LOGICAL-c389t-7a49096f04d8a3ce48f5b6df54e8705f58320876af2c40aaab36ab3128244f6f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12589431$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-03274468$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Viala, J</creatorcontrib><creatorcontrib>Mazodier, P</creatorcontrib><title>The ATPase ClpX is conditionally involved in the morphological differentiation of Streptomyces lividans</title><title>Molecular genetics and genomics : MGG</title><addtitle>Mol Genet Genomics</addtitle><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.</description><subject>Adenosine Triphosphatases</subject><subject>Adenosine Triphosphatases - genetics</subject><subject>Adenosine Triphosphatases - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Antibiotics</subject><subject>ATPases Associated with Diverse Cellular Activities</subject><subject>Bacteria</subject><subject>Bacterial Proteins</subject><subject>Base Sequence</subject><subject>Cell Cycle</subject><subject>E coli</subject><subject>Endopeptidase Clp</subject><subject>Escherichia coli Proteins</subject><subject>Gene Expression</subject><subject>Genes</subject><subject>Genes, Bacterial</subject><subject>Genetic Complementation Test</subject><subject>Genomes</subject><subject>Genomics</subject><subject>Genotype & phenotype</subject><subject>Hydrogen-Ion Concentration</subject><subject>Life Sciences</subject><subject>Molecular Chaperones</subject><subject>Molecular Sequence Data</subject><subject>Morphology</subject><subject>Mutation</subject><subject>Phenotype</subject><subject>Plasmids</subject><subject>Plasmids - 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Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Molecular genetics and genomics : MGG</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Viala, J</au><au>Mazodier, P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The ATPase ClpX is conditionally involved in the morphological differentiation of Streptomyces lividans</atitle><jtitle>Molecular genetics and genomics : MGG</jtitle><addtitle>Mol Genet Genomics</addtitle><date>2003-02</date><risdate>2003</risdate><volume>268</volume><issue>5</issue><spage>563</spage><epage>569</epage><pages>563-569</pages><issn>1617-4615</issn><eissn>1617-4623</eissn><abstract>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.</abstract><cop>Germany</cop><pub>Springer Nature B.V</pub><pmid>12589431</pmid><doi>10.1007/s00438-002-0783-1</doi><tpages>7</tpages></addata></record> |
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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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