Alteration of the synthesis of the Clp ATP‐dependent protease affects morphological and physiological differentiation in Streptomyces
The genes of Streptomyces coelicolor A3(2) encoding catalytic subunits (ClpP) and regulatory subunits (ClpX and ClpC) of the ATP‐dependent protease family Clp were cloned, mapped and characterized. S. coelicolor contains at least two clpP genes, clpP1 and clpP2, located in tandem upstream from the c...
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| Veröffentlicht in: | Molecular microbiology 1999-05, Vol.32 (3), p.505-517 |
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| creator | De Crécy‐Lagard, Valérie Servant‐Moisson, Pascale Viala, Julie Grandvalet, Cosette Mazodier, Philippe |
| description | The genes of Streptomyces coelicolor A3(2) encoding catalytic subunits (ClpP) and regulatory subunits (ClpX and ClpC) of the ATP‐dependent protease family Clp were cloned, mapped and characterized. S. coelicolor contains at least two clpP genes, clpP1 and clpP2, located in tandem upstream from the clpX gene, and at least two unlinked clpC genes. Disruption of the clpP1 gene in S. lividans and S. coelicolor blocks differentiation at the substrate mycelium step. Overexpression of clpP1 and clpP2 accelerates aerial mycelium formation in S. lividans, S. albus and S. coelicolor. Overproduction of ClpX accelerates actinorhodin production in S. coelicolor and activates its production in S. lividans. |
| doi_str_mv | 10.1046/j.1365-2958.1999.01364.x |
| format | Article |
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S. coelicolor contains at least two clpP genes, clpP1 and clpP2, located in tandem upstream from the clpX gene, and at least two unlinked clpC genes. Disruption of the clpP1 gene in S. lividans and S. coelicolor blocks differentiation at the substrate mycelium step. Overexpression of clpP1 and clpP2 accelerates aerial mycelium formation in S. lividans, S. albus and S. coelicolor. Overproduction of ClpX accelerates actinorhodin production in S. coelicolor and activates its production in S. lividans.</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1046/j.1365-2958.1999.01364.x</identifier><identifier>PMID: 10320574</identifier><language>eng</language><publisher>Oxford BSL: Blackwell Science Ltd</publisher><subject>Adenosine Triphosphatases ; Adenosine Triphosphatases - genetics ; Adenosine Triphosphatases - metabolism ; Amino Acid Sequence ; Bacterial Proteins ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Base Sequence ; Biochemistry, Molecular Biology ; Chromosome Mapping ; Endopeptidase Clp ; Gene Expression Regulation, Bacterial ; Genes, Bacterial ; Life Sciences ; Molecular Sequence Data ; Peptide Hydrolases ; Peptide Hydrolases - metabolism ; Protein Processing, Post-Translational ; Sequence Homology, Amino Acid ; Serine Endopeptidases ; Serine Endopeptidases - genetics ; Serine Endopeptidases - metabolism ; Species Specificity ; Streptomyces ; Streptomyces - classification ; Streptomyces - cytology ; Streptomyces - physiology ; Streptomyces coelicolor ; Transcription, Genetic</subject><ispartof>Molecular microbiology, 1999-05, Vol.32 (3), p.505-517</ispartof><rights>Blackwell Science Ltd, Oxford</rights><rights>Copyright Blackwell Scientific Publications Ltd. May 1999</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5234-895b28a5d5e58475d661c7b6c1258879720632b9cbe7a302c35ce64531d84f53</citedby><cites>FETCH-LOGICAL-c5234-895b28a5d5e58475d661c7b6c1258879720632b9cbe7a302c35ce64531d84f53</cites><orcidid>0000-0002-1687-455X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1046%2Fj.1365-2958.1999.01364.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1046%2Fj.1365-2958.1999.01364.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>230,314,776,780,881,1411,1427,27901,27902,45550,45551,46384,46808</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10320574$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-03140074$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>De Crécy‐Lagard, Valérie</creatorcontrib><creatorcontrib>Servant‐Moisson, Pascale</creatorcontrib><creatorcontrib>Viala, Julie</creatorcontrib><creatorcontrib>Grandvalet, Cosette</creatorcontrib><creatorcontrib>Mazodier, Philippe</creatorcontrib><title>Alteration of the synthesis of the Clp ATP‐dependent protease affects morphological and physiological differentiation in Streptomyces</title><title>Molecular microbiology</title><addtitle>Mol Microbiol</addtitle><description>The genes of Streptomyces coelicolor A3(2) encoding catalytic subunits (ClpP) and regulatory subunits (ClpX and ClpC) of the ATP‐dependent protease family Clp were cloned, mapped and characterized. S. coelicolor contains at least two clpP genes, clpP1 and clpP2, located in tandem upstream from the clpX gene, and at least two unlinked clpC genes. Disruption of the clpP1 gene in S. lividans and S. coelicolor blocks differentiation at the substrate mycelium step. Overexpression of clpP1 and clpP2 accelerates aerial mycelium formation in S. lividans, S. albus and S. coelicolor. Overproduction of ClpX accelerates actinorhodin production in S. coelicolor and activates its production in S. lividans.</description><subject>Adenosine Triphosphatases</subject><subject>Adenosine Triphosphatases - genetics</subject><subject>Adenosine Triphosphatases - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Bacterial Proteins</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Base Sequence</subject><subject>Biochemistry, Molecular Biology</subject><subject>Chromosome Mapping</subject><subject>Endopeptidase Clp</subject><subject>Gene Expression Regulation, Bacterial</subject><subject>Genes, Bacterial</subject><subject>Life Sciences</subject><subject>Molecular Sequence Data</subject><subject>Peptide Hydrolases</subject><subject>Peptide Hydrolases - metabolism</subject><subject>Protein Processing, Post-Translational</subject><subject>Sequence Homology, Amino Acid</subject><subject>Serine Endopeptidases</subject><subject>Serine Endopeptidases - genetics</subject><subject>Serine Endopeptidases - metabolism</subject><subject>Species Specificity</subject><subject>Streptomyces</subject><subject>Streptomyces - classification</subject><subject>Streptomyces - cytology</subject><subject>Streptomyces - physiology</subject><subject>Streptomyces coelicolor</subject><subject>Transcription, Genetic</subject><issn>0950-382X</issn><issn>1365-2958</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkb2O1DAUhS0EYmcXXgFZFEgUCXb8FxcUoxHsrjQrkJiCznIch_EoiYOdWTYdHS3PyJPgkGWEaKC69vV3zvXVAQBilGNE-atDjglnWSFZmWMpZY7SneZ3D8Dq9PAQrJBkKCNl8fEMnMd4QIlCnDwGZxiRAjFBV-Dbuh1t0KPzPfQNHPcWxqlPJbr4u7FpB7jevf_x9XttB9vXth_hEPxodbRQN401Y4SdD8Pet_6TM7qFuq_hsJ-iO3Vql8CQpG4Z5nr4YQx2GH03GRufgEeNbqN9el8vwO7tm93mKtu-u7zerLeZYQWhWSlZVZSa1cyykgpWc46NqLjBBStLIUWRFiwqaSorNEGFIcxYThnBdUkbRi7Ay8V2r1s1BNfpMCmvnbpab9XcQwRThAS9xYl9sbBp189HG0fVuWhs2-re-mNUXAqGhUD_BLEgCFEyg8__Ag_-GPq0r8KSM5xm8wSVC2SCjzHY5vRPjNScvjqoOWQ1h6zm9NWv9NVdkj679z9Wna3_EC5xJ-D1AnxxrZ3-21jd3FzPJ_IT1nO_Jg</recordid><startdate>199905</startdate><enddate>199905</enddate><creator>De Crécy‐Lagard, Valérie</creator><creator>Servant‐Moisson, Pascale</creator><creator>Viala, Julie</creator><creator>Grandvalet, Cosette</creator><creator>Mazodier, Philippe</creator><general>Blackwell Science Ltd</general><general>Blackwell Publishing Ltd</general><general>Wiley</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0002-1687-455X</orcidid></search><sort><creationdate>199905</creationdate><title>Alteration of the synthesis of the Clp ATP‐dependent protease affects morphological and physiological differentiation in Streptomyces</title><author>De Crécy‐Lagard, Valérie ; Servant‐Moisson, Pascale ; Viala, Julie ; Grandvalet, Cosette ; Mazodier, Philippe</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5234-895b28a5d5e58475d661c7b6c1258879720632b9cbe7a302c35ce64531d84f53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Adenosine Triphosphatases</topic><topic>Adenosine Triphosphatases - genetics</topic><topic>Adenosine Triphosphatases - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Bacterial Proteins</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Base Sequence</topic><topic>Biochemistry, Molecular Biology</topic><topic>Chromosome Mapping</topic><topic>Endopeptidase Clp</topic><topic>Gene Expression Regulation, Bacterial</topic><topic>Genes, Bacterial</topic><topic>Life Sciences</topic><topic>Molecular Sequence Data</topic><topic>Peptide Hydrolases</topic><topic>Peptide Hydrolases - metabolism</topic><topic>Protein Processing, Post-Translational</topic><topic>Sequence Homology, Amino Acid</topic><topic>Serine Endopeptidases</topic><topic>Serine Endopeptidases - genetics</topic><topic>Serine Endopeptidases - metabolism</topic><topic>Species Specificity</topic><topic>Streptomyces</topic><topic>Streptomyces - classification</topic><topic>Streptomyces - cytology</topic><topic>Streptomyces - physiology</topic><topic>Streptomyces coelicolor</topic><topic>Transcription, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>De Crécy‐Lagard, Valérie</creatorcontrib><creatorcontrib>Servant‐Moisson, Pascale</creatorcontrib><creatorcontrib>Viala, Julie</creatorcontrib><creatorcontrib>Grandvalet, Cosette</creatorcontrib><creatorcontrib>Mazodier, Philippe</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Molecular microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>De Crécy‐Lagard, Valérie</au><au>Servant‐Moisson, Pascale</au><au>Viala, Julie</au><au>Grandvalet, Cosette</au><au>Mazodier, Philippe</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Alteration of the synthesis of the Clp ATP‐dependent protease affects morphological and physiological differentiation in Streptomyces</atitle><jtitle>Molecular microbiology</jtitle><addtitle>Mol Microbiol</addtitle><date>1999-05</date><risdate>1999</risdate><volume>32</volume><issue>3</issue><spage>505</spage><epage>517</epage><pages>505-517</pages><issn>0950-382X</issn><eissn>1365-2958</eissn><abstract>The genes of Streptomyces coelicolor A3(2) encoding catalytic subunits (ClpP) and regulatory subunits (ClpX and ClpC) of the ATP‐dependent protease family Clp were cloned, mapped and characterized. S. coelicolor contains at least two clpP genes, clpP1 and clpP2, located in tandem upstream from the clpX gene, and at least two unlinked clpC genes. Disruption of the clpP1 gene in S. lividans and S. coelicolor blocks differentiation at the substrate mycelium step. Overexpression of clpP1 and clpP2 accelerates aerial mycelium formation in S. lividans, S. albus and S. coelicolor. Overproduction of ClpX accelerates actinorhodin production in S. coelicolor and activates its production in S. lividans.</abstract><cop>Oxford BSL</cop><pub>Blackwell Science Ltd</pub><pmid>10320574</pmid><doi>10.1046/j.1365-2958.1999.01364.x</doi><tpages>13</tpages><orcidid>https://orcid.org/0000-0002-1687-455X</orcidid></addata></record> |
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| ispartof | Molecular microbiology, 1999-05, Vol.32 (3), p.505-517 |
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| subjects | Adenosine Triphosphatases Adenosine Triphosphatases - genetics Adenosine Triphosphatases - metabolism Amino Acid Sequence Bacterial Proteins Bacterial Proteins - genetics Bacterial Proteins - metabolism Base Sequence Biochemistry, Molecular Biology Chromosome Mapping Endopeptidase Clp Gene Expression Regulation, Bacterial Genes, Bacterial Life Sciences Molecular Sequence Data Peptide Hydrolases Peptide Hydrolases - metabolism Protein Processing, Post-Translational Sequence Homology, Amino Acid Serine Endopeptidases Serine Endopeptidases - genetics Serine Endopeptidases - metabolism Species Specificity Streptomyces Streptomyces - classification Streptomyces - cytology Streptomyces - physiology Streptomyces coelicolor Transcription, Genetic |
| title | Alteration of the synthesis of the Clp ATP‐dependent protease affects morphological and physiological differentiation in Streptomyces |
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