Loss of Pseudomonas aeruginosa PhpA aminopeptidase activity results in increased algD transcription
Inactivation of Pseudomonas aeruginosa phpA, encoding a putative leucine aminopeptidase, results in increased transcription of algD. The homologous protein in Escherichia coli, PepA, is multifunctional, possessing independent aminopeptidase and DNA-binding activities. Here we provide in vitro eviden...
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| Veröffentlicht in: | Journal of bacteriology 2001-08, Vol.183 (15), p.4674-4679 |
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| container_end_page | 4679 |
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| container_issue | 15 |
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| container_title | Journal of bacteriology |
| container_volume | 183 |
| creator | Woolwine, S C Sprinkle, A B Wozniak, D J |
| description | Inactivation of Pseudomonas aeruginosa phpA, encoding a putative leucine aminopeptidase, results in increased transcription of algD. The homologous protein in Escherichia coli, PepA, is multifunctional, possessing independent aminopeptidase and DNA-binding activities. Here we provide in vitro evidence that PhpA is an aminopeptidase and show that this activity is the relevant property with regard to algD expression. This regulation occurred at the previously mapped algD transcription initiation site and was not due to activation of an alternative promoter. |
| doi_str_mv | 10.1128/JB.183.15.4674-4679.2001 |
| format | Article |
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The homologous protein in Escherichia coli, PepA, is multifunctional, possessing independent aminopeptidase and DNA-binding activities. Here we provide in vitro evidence that PhpA is an aminopeptidase and show that this activity is the relevant property with regard to algD expression. This regulation occurred at the previously mapped algD transcription initiation site and was not due to activation of an alternative promoter.</description><identifier>ISSN: 0021-9193</identifier><identifier>EISSN: 1098-5530</identifier><identifier>DOI: 10.1128/JB.183.15.4674-4679.2001</identifier><identifier>PMID: 11443106</identifier><identifier>CODEN: JOBAAY</identifier><language>eng</language><publisher>United States: American Society for Microbiology</publisher><subject>Bacteria ; Bacteriology ; Carbohydrate Dehydrogenases - genetics ; Gene Expression Regulation, Bacterial ; Gene Expression Regulation, Enzymologic ; Genetics and Molecular Biology ; Leucyl Aminopeptidase - genetics ; Leucyl Aminopeptidase - metabolism ; Mutagenesis ; Promoter Regions, Genetic ; Pseudomonas aeruginosa - enzymology ; Pseudomonas aeruginosa - genetics ; Transcription, Genetic</subject><ispartof>Journal of bacteriology, 2001-08, Vol.183 (15), p.4674-4679</ispartof><rights>Copyright American Society for Microbiology Aug 2001</rights><rights>Copyright © 2001, American Society for Microbiology 2001</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c441t-d0bdbb31666fef8820b300cbf201a9732f0ab317cdadc1f181e117d5fe8bb373</citedby><cites>FETCH-LOGICAL-c441t-d0bdbb31666fef8820b300cbf201a9732f0ab317cdadc1f181e117d5fe8bb373</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC95366/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC95366/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11443106$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Woolwine, S C</creatorcontrib><creatorcontrib>Sprinkle, A B</creatorcontrib><creatorcontrib>Wozniak, D J</creatorcontrib><title>Loss of Pseudomonas aeruginosa PhpA aminopeptidase activity results in increased algD transcription</title><title>Journal of bacteriology</title><addtitle>J Bacteriol</addtitle><description>Inactivation of Pseudomonas aeruginosa phpA, encoding a putative leucine aminopeptidase, results in increased transcription of algD. The homologous protein in Escherichia coli, PepA, is multifunctional, possessing independent aminopeptidase and DNA-binding activities. Here we provide in vitro evidence that PhpA is an aminopeptidase and show that this activity is the relevant property with regard to algD expression. This regulation occurred at the previously mapped algD transcription initiation site and was not due to activation of an alternative promoter.</description><subject>Bacteria</subject><subject>Bacteriology</subject><subject>Carbohydrate Dehydrogenases - genetics</subject><subject>Gene Expression Regulation, Bacterial</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>Genetics and Molecular Biology</subject><subject>Leucyl Aminopeptidase - genetics</subject><subject>Leucyl Aminopeptidase - metabolism</subject><subject>Mutagenesis</subject><subject>Promoter Regions, Genetic</subject><subject>Pseudomonas aeruginosa - enzymology</subject><subject>Pseudomonas aeruginosa - genetics</subject><subject>Transcription, Genetic</subject><issn>0021-9193</issn><issn>1098-5530</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkVtrGzEQhUVoiF0nf6GIvu9GI-1FC31J0iRtMCQPeRdaXWwFe7WVdgP-9x0T0wuI0Yg533DQIYQCKwG4vH66LUGKEuqyatqqwNKVnDE4I0tgnSzqWrBPZMkYh6KDTizI55zfUFBVNb8gC8BGAGuWxKxjzjR6-pLdbOM-DjpT7dK8CUPMmr5sxxuq9_gY3TgFq7Oj2kzhPUwHmlyed1OmYcBjksOhpXq3-U6npIdsUkAkDpfk3Otddlene0VeH-5f734U6-fHn3c368JUFUyFZb3tewFN03jnpeSsF4yZ3nMGumsF90zjuDVWWwMeJDiA1tbeScRasSLfPtaOc7931rgBXezUmMJep4OKOqj_J0PYqk18V10tmgbxryc8xV-zy5N6i3Ma0LDivGWtRA2K5IfIJPy35Pyf9cDUMRr1dKswGgW1OkZzLJ06RoPol3_t_QVPWYjfkZ6OJQ</recordid><startdate>20010801</startdate><enddate>20010801</enddate><creator>Woolwine, S C</creator><creator>Sprinkle, A B</creator><creator>Wozniak, D J</creator><general>American Society for Microbiology</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>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>5PM</scope></search><sort><creationdate>20010801</creationdate><title>Loss of Pseudomonas aeruginosa PhpA aminopeptidase activity results in increased algD transcription</title><author>Woolwine, S C ; Sprinkle, A B ; Wozniak, D J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c441t-d0bdbb31666fef8820b300cbf201a9732f0ab317cdadc1f181e117d5fe8bb373</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Bacteria</topic><topic>Bacteriology</topic><topic>Carbohydrate Dehydrogenases - genetics</topic><topic>Gene Expression Regulation, Bacterial</topic><topic>Gene Expression Regulation, Enzymologic</topic><topic>Genetics and Molecular Biology</topic><topic>Leucyl Aminopeptidase - genetics</topic><topic>Leucyl Aminopeptidase - metabolism</topic><topic>Mutagenesis</topic><topic>Promoter Regions, Genetic</topic><topic>Pseudomonas aeruginosa - enzymology</topic><topic>Pseudomonas aeruginosa - genetics</topic><topic>Transcription, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Woolwine, S C</creatorcontrib><creatorcontrib>Sprinkle, A B</creatorcontrib><creatorcontrib>Wozniak, D J</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>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>PubMed Central (Full Participant titles)</collection><jtitle>Journal of bacteriology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Woolwine, S C</au><au>Sprinkle, A B</au><au>Wozniak, D J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Loss of Pseudomonas aeruginosa PhpA aminopeptidase activity results in increased algD transcription</atitle><jtitle>Journal of bacteriology</jtitle><addtitle>J Bacteriol</addtitle><date>2001-08-01</date><risdate>2001</risdate><volume>183</volume><issue>15</issue><spage>4674</spage><epage>4679</epage><pages>4674-4679</pages><issn>0021-9193</issn><eissn>1098-5530</eissn><coden>JOBAAY</coden><abstract>Inactivation of Pseudomonas aeruginosa phpA, encoding a putative leucine aminopeptidase, results in increased transcription of algD. The homologous protein in Escherichia coli, PepA, is multifunctional, possessing independent aminopeptidase and DNA-binding activities. Here we provide in vitro evidence that PhpA is an aminopeptidase and show that this activity is the relevant property with regard to algD expression. This regulation occurred at the previously mapped algD transcription initiation site and was not due to activation of an alternative promoter.</abstract><cop>United States</cop><pub>American Society for Microbiology</pub><pmid>11443106</pmid><doi>10.1128/JB.183.15.4674-4679.2001</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | Bacteria Bacteriology Carbohydrate Dehydrogenases - genetics Gene Expression Regulation, Bacterial Gene Expression Regulation, Enzymologic Genetics and Molecular Biology Leucyl Aminopeptidase - genetics Leucyl Aminopeptidase - metabolism Mutagenesis Promoter Regions, Genetic Pseudomonas aeruginosa - enzymology Pseudomonas aeruginosa - genetics Transcription, Genetic |
| title | Loss of Pseudomonas aeruginosa PhpA aminopeptidase activity results in increased algD transcription |
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