The expression of selected non-ribosomal peptide synthetases in Aspergillus fumigatus is controlled by the availability of free iron
Three non-ribosomal peptide synthetase genes, termed sidD, sidC and sidE, have been identified in Aspergillus fumigatus. Gene expression analysis by RT-PCR confirms that expression of both sidD and C was reduced by up to 90% under iron-replete conditions indicative of a likely role in siderophore bi...
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| Veröffentlicht in: | FEMS microbiology letters 2005-07, Vol.248 (1), p.83-91 |
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| creator | Reiber, Kathrin Reeves, Emer P. Neville, Claire M. Winkler, Robert Gebhardt, Peter Kavanagh, Kevin Doyle, Sean |
| description | Three non-ribosomal peptide synthetase genes, termed
sidD,
sidC and
sidE, have been identified in
Aspergillus fumigatus. Gene expression analysis by RT-PCR confirms that expression of both
sidD and
C was reduced by up to 90% under iron-replete conditions indicative of a likely role in siderophore biosynthesis.
SidE expression was less sensitive to iron levels. In addition, two proteins purified from mycelia grown under iron-limiting conditions corresponded to SidD (∼200
kDa) and SidC (496
kDa) as determined by MALDI ToF peptide mass fingerprinting and MALDI LIFT-ToF/ToF. Siderophore synthetases are unique in bacteria and fungi and represent an attractive target for antimicrobial chemotherapy. |
| doi_str_mv | 10.1016/j.femsle.2005.05.028 |
| format | Article |
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sidD,
sidC and
sidE, have been identified in
Aspergillus fumigatus. Gene expression analysis by RT-PCR confirms that expression of both
sidD and
C was reduced by up to 90% under iron-replete conditions indicative of a likely role in siderophore biosynthesis.
SidE expression was less sensitive to iron levels. In addition, two proteins purified from mycelia grown under iron-limiting conditions corresponded to SidD (∼200
kDa) and SidC (496
kDa) as determined by MALDI ToF peptide mass fingerprinting and MALDI LIFT-ToF/ToF. Siderophore synthetases are unique in bacteria and fungi and represent an attractive target for antimicrobial chemotherapy.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1016/j.femsle.2005.05.028</identifier><identifier>PMID: 15953695</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Elsevier B.V</publisher><subject>4′-PPTase ; Aspergillus fumigatus - enzymology ; Aspergillus fumigatus - genetics ; Aspergillus fumigatus - physiology ; Biological and medical sciences ; Fundamental and applied biological sciences. Psychology ; Growth, nutrition, metabolism, transports, enzymes. Molecular biology ; Iron ; Iron - chemistry ; Iron - metabolism ; MALDI ToF ; Microbiology ; Mycology ; NRPS ; Peptide Synthases - genetics ; Peptide Synthases - metabolism ; Proteomics ; Reverse Transcriptase Polymerase Chain Reaction ; Secondary metabolites ; Siderophore ; Siderophores - metabolism ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><ispartof>FEMS microbiology letters, 2005-07, Vol.248 (1), p.83-91</ispartof><rights>2005 Federation of European Microbiological Societies</rights><rights>2005 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3843-3ab48c7a5c8d9b3e8f2dae9b9810fab856586f6e934ad4e54e7de3552b4baf9c3</citedby><cites>FETCH-LOGICAL-c3843-3ab48c7a5c8d9b3e8f2dae9b9810fab856586f6e934ad4e54e7de3552b4baf9c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.femsle.2005.05.028$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1016%2Fj.femsle.2005.05.028$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16884127$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15953695$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Reiber, Kathrin</creatorcontrib><creatorcontrib>Reeves, Emer P.</creatorcontrib><creatorcontrib>Neville, Claire M.</creatorcontrib><creatorcontrib>Winkler, Robert</creatorcontrib><creatorcontrib>Gebhardt, Peter</creatorcontrib><creatorcontrib>Kavanagh, Kevin</creatorcontrib><creatorcontrib>Doyle, Sean</creatorcontrib><title>The expression of selected non-ribosomal peptide synthetases in Aspergillus fumigatus is controlled by the availability of free iron</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>Three non-ribosomal peptide synthetase genes, termed
sidD,
sidC and
sidE, have been identified in
Aspergillus fumigatus. Gene expression analysis by RT-PCR confirms that expression of both
sidD and
C was reduced by up to 90% under iron-replete conditions indicative of a likely role in siderophore biosynthesis.
SidE expression was less sensitive to iron levels. In addition, two proteins purified from mycelia grown under iron-limiting conditions corresponded to SidD (∼200
kDa) and SidC (496
kDa) as determined by MALDI ToF peptide mass fingerprinting and MALDI LIFT-ToF/ToF. Siderophore synthetases are unique in bacteria and fungi and represent an attractive target for antimicrobial chemotherapy.</description><subject>4′-PPTase</subject><subject>Aspergillus fumigatus - enzymology</subject><subject>Aspergillus fumigatus - genetics</subject><subject>Aspergillus fumigatus - physiology</subject><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Growth, nutrition, metabolism, transports, enzymes. Molecular biology</subject><subject>Iron</subject><subject>Iron - chemistry</subject><subject>Iron - metabolism</subject><subject>MALDI ToF</subject><subject>Microbiology</subject><subject>Mycology</subject><subject>NRPS</subject><subject>Peptide Synthases - genetics</subject><subject>Peptide Synthases - metabolism</subject><subject>Proteomics</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>Secondary metabolites</subject><subject>Siderophore</subject><subject>Siderophores - metabolism</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkUFv1DAQhSMEotvCP0DIF7hlsRPbcS5IVUUp0iIu5Ww5zrj1yomDJ2nJnR9OQlbqDZBGmjl8741mXpa9YXTPKJMfjnsHHQbYF5SK_VqFepbtmKh4Lmupnmc7WlYqZ7SuzrJzxCOllBdUvszOmKhFKWuxy37d3gOBn0MCRB97Eh1BCGBHaEkf-zz5JmLsTCADDKNvgeDcj_cwGgQkvieXOEC68yFMSNzU-TszLpNHYmM_phjCYtTMZJEQ82B8MI0PfpzXRS4BEJ9i_yp74UxAeH3qF9n360-3Vzf54dvnL1eXh9yWipd5aRqubGWEVW3dlKBc0Rqom1ox6kyjhBRKOgl1yU3LQXCoWiiFKBreGFfb8iJ7v_kOKf6YAEfdebQQgukhTqhltbylouyfIKtkwXmhFpBvoE0RMYHTQ_KdSbNmVK8x6aPeYtJrTHqtP7K3J_-p6aB9Ep1yWYB3J8CgNcEl01uPT5xUirOiWrhq4x59gPm_luvrrwdVLsqPmxKWhz94SBqth95C69MSv26j__sNvwE43cfR</recordid><startdate>200507</startdate><enddate>200507</enddate><creator>Reiber, Kathrin</creator><creator>Reeves, Emer P.</creator><creator>Neville, Claire M.</creator><creator>Winkler, Robert</creator><creator>Gebhardt, Peter</creator><creator>Kavanagh, Kevin</creator><creator>Doyle, Sean</creator><general>Elsevier B.V</general><general>Blackwell Publishing Ltd</general><general>Blackwell</general><scope>IQODW</scope><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>7TM</scope><scope>M7N</scope><scope>7X8</scope></search><sort><creationdate>200507</creationdate><title>The expression of selected non-ribosomal peptide synthetases in Aspergillus fumigatus is controlled by the availability of free iron</title><author>Reiber, Kathrin ; Reeves, Emer P. ; Neville, Claire M. ; Winkler, Robert ; Gebhardt, Peter ; Kavanagh, Kevin ; Doyle, Sean</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3843-3ab48c7a5c8d9b3e8f2dae9b9810fab856586f6e934ad4e54e7de3552b4baf9c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>4′-PPTase</topic><topic>Aspergillus fumigatus - enzymology</topic><topic>Aspergillus fumigatus - genetics</topic><topic>Aspergillus fumigatus - physiology</topic><topic>Biological and medical sciences</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Growth, nutrition, metabolism, transports, enzymes. Molecular biology</topic><topic>Iron</topic><topic>Iron - chemistry</topic><topic>Iron - metabolism</topic><topic>MALDI ToF</topic><topic>Microbiology</topic><topic>Mycology</topic><topic>NRPS</topic><topic>Peptide Synthases - genetics</topic><topic>Peptide Synthases - metabolism</topic><topic>Proteomics</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>Secondary metabolites</topic><topic>Siderophore</topic><topic>Siderophores - metabolism</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Reiber, Kathrin</creatorcontrib><creatorcontrib>Reeves, Emer P.</creatorcontrib><creatorcontrib>Neville, Claire M.</creatorcontrib><creatorcontrib>Winkler, Robert</creatorcontrib><creatorcontrib>Gebhardt, Peter</creatorcontrib><creatorcontrib>Kavanagh, Kevin</creatorcontrib><creatorcontrib>Doyle, Sean</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Reiber, Kathrin</au><au>Reeves, Emer P.</au><au>Neville, Claire M.</au><au>Winkler, Robert</au><au>Gebhardt, Peter</au><au>Kavanagh, Kevin</au><au>Doyle, Sean</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The expression of selected non-ribosomal peptide synthetases in Aspergillus fumigatus is controlled by the availability of free iron</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>2005-07</date><risdate>2005</risdate><volume>248</volume><issue>1</issue><spage>83</spage><epage>91</epage><pages>83-91</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><coden>FMLED7</coden><abstract>Three non-ribosomal peptide synthetase genes, termed
sidD,
sidC and
sidE, have been identified in
Aspergillus fumigatus. Gene expression analysis by RT-PCR confirms that expression of both
sidD and
C was reduced by up to 90% under iron-replete conditions indicative of a likely role in siderophore biosynthesis.
SidE expression was less sensitive to iron levels. In addition, two proteins purified from mycelia grown under iron-limiting conditions corresponded to SidD (∼200
kDa) and SidC (496
kDa) as determined by MALDI ToF peptide mass fingerprinting and MALDI LIFT-ToF/ToF. Siderophore synthetases are unique in bacteria and fungi and represent an attractive target for antimicrobial chemotherapy.</abstract><cop>Oxford, UK</cop><pub>Elsevier B.V</pub><pmid>15953695</pmid><doi>10.1016/j.femsle.2005.05.028</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0378-1097 |
| ispartof | FEMS microbiology letters, 2005-07, Vol.248 (1), p.83-91 |
| issn | 0378-1097 1574-6968 |
| language | eng |
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| source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
| subjects | 4′-PPTase Aspergillus fumigatus - enzymology Aspergillus fumigatus - genetics Aspergillus fumigatus - physiology Biological and medical sciences Fundamental and applied biological sciences. Psychology Growth, nutrition, metabolism, transports, enzymes. Molecular biology Iron Iron - chemistry Iron - metabolism MALDI ToF Microbiology Mycology NRPS Peptide Synthases - genetics Peptide Synthases - metabolism Proteomics Reverse Transcriptase Polymerase Chain Reaction Secondary metabolites Siderophore Siderophores - metabolism Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization |
| title | The expression of selected non-ribosomal peptide synthetases in Aspergillus fumigatus is controlled by the availability of free iron |
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