Phosphoprotein affinity purification identifies proteins involved in S-adenosyl-L-methionine-induced enhancement of antibiotic production in Streptomyces coelicolor
Streptomycetes are the major natural source of clinical antibiotics. The enhanced secondary metabolite production of many streptomycetes by S -adenosylmethionine (SAM) in previous studies suggested the existence of a common SAM regulatory effect. We screened nine proteins using the phosphoprotein pu...
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| Veröffentlicht in: | Journal of antibiotics 2011-01, Vol.64 (1), p.97-101 |
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| creator | Meng, Lingzhu Yang, Seung Hwan Palaniyandi, Sasikumar Arunachalam Lee, Sung-Kwon Lee, In-Ae Kim, Tae-Jong Suh, Joo-Won |
| description | Streptomycetes are the major natural source of clinical antibiotics. The enhanced secondary metabolite production of many streptomycetes by
S
-adenosylmethionine (SAM) in previous studies suggested the existence of a common SAM regulatory effect. We screened nine proteins using the phosphoprotein purification column from
Streptomyces coelicolor
. Among them, genes (SCO5477, SCO5113, SCO4647, SCO4885 and SCO1793) for five proteins were disrupted by insertion mutation. The undecylprodigiosin and actinorhodin productions were changed in all mutations. The SAM-induced enhancement of actinorhodin production was abolished by all mutations except SCO4885 mutation, which reduced the production of actinorhodin and undecylprodigiosin with SAM treatment. This study demonstrates that phosphoprotein affinity purification can be used as a screening method to identify the proteins involved SAM signaling. |
| doi_str_mv | 10.1038/ja.2010.148 |
| format | Article |
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S
-adenosylmethionine (SAM) in previous studies suggested the existence of a common SAM regulatory effect. We screened nine proteins using the phosphoprotein purification column from
Streptomyces coelicolor
. Among them, genes (SCO5477, SCO5113, SCO4647, SCO4885 and SCO1793) for five proteins were disrupted by insertion mutation. The undecylprodigiosin and actinorhodin productions were changed in all mutations. The SAM-induced enhancement of actinorhodin production was abolished by all mutations except SCO4885 mutation, which reduced the production of actinorhodin and undecylprodigiosin with SAM treatment. This study demonstrates that phosphoprotein affinity purification can be used as a screening method to identify the proteins involved SAM signaling.</description><identifier>ISSN: 0021-8820</identifier><identifier>EISSN: 1881-1469</identifier><identifier>DOI: 10.1038/ja.2010.148</identifier><identifier>PMID: 21139623</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/208/737 ; 631/326/22/1290 ; 631/80/86 ; 631/92/60 ; Anti-Bacterial Agents - biosynthesis ; Antibiotics ; Bacterial Proteins - biosynthesis ; Bacterial Proteins - genetics ; Bacterial Proteins - isolation & purification ; Bacteriology ; Biomedical and Life Sciences ; Bioorganic Chemistry ; Chromatography, Affinity ; DNA, Bacterial - genetics ; Gene Expression Regulation, Bacterial ; Life Sciences ; Medicinal Chemistry ; Metabolites ; Microbiology ; Mutagenesis, Insertional ; Mutation ; Organic Chemistry ; original-article ; Phosphoproteins - chemistry ; Phosphoproteins - metabolism ; Proteins ; S-Adenosylmethionine - pharmacology ; Streptomyces coelicolor - drug effects ; Streptomyces coelicolor - genetics ; Streptomyces coelicolor - metabolism ; Tandem Mass Spectrometry</subject><ispartof>Journal of antibiotics, 2011-01, Vol.64 (1), p.97-101</ispartof><rights>Japan Antibiotics Research Association 2011</rights><rights>Copyright Nature Publishing Group Jan 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c419t-77f4903069e181f5772f75af351055ae6f2003a25e8a683c4a1fab664aa5e5d93</citedby><cites>FETCH-LOGICAL-c419t-77f4903069e181f5772f75af351055ae6f2003a25e8a683c4a1fab664aa5e5d93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21139623$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Meng, Lingzhu</creatorcontrib><creatorcontrib>Yang, Seung Hwan</creatorcontrib><creatorcontrib>Palaniyandi, Sasikumar Arunachalam</creatorcontrib><creatorcontrib>Lee, Sung-Kwon</creatorcontrib><creatorcontrib>Lee, In-Ae</creatorcontrib><creatorcontrib>Kim, Tae-Jong</creatorcontrib><creatorcontrib>Suh, Joo-Won</creatorcontrib><title>Phosphoprotein affinity purification identifies proteins involved in S-adenosyl-L-methionine-induced enhancement of antibiotic production in Streptomyces coelicolor</title><title>Journal of antibiotics</title><addtitle>J Antibiot</addtitle><addtitle>J Antibiot (Tokyo)</addtitle><description>Streptomycetes are the major natural source of clinical antibiotics. The enhanced secondary metabolite production of many streptomycetes by
S
-adenosylmethionine (SAM) in previous studies suggested the existence of a common SAM regulatory effect. We screened nine proteins using the phosphoprotein purification column from
Streptomyces coelicolor
. Among them, genes (SCO5477, SCO5113, SCO4647, SCO4885 and SCO1793) for five proteins were disrupted by insertion mutation. The undecylprodigiosin and actinorhodin productions were changed in all mutations. The SAM-induced enhancement of actinorhodin production was abolished by all mutations except SCO4885 mutation, which reduced the production of actinorhodin and undecylprodigiosin with SAM treatment. This study demonstrates that phosphoprotein affinity purification can be used as a screening method to identify the proteins involved SAM signaling.</description><subject>631/208/737</subject><subject>631/326/22/1290</subject><subject>631/80/86</subject><subject>631/92/60</subject><subject>Anti-Bacterial Agents - biosynthesis</subject><subject>Antibiotics</subject><subject>Bacterial Proteins - biosynthesis</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - isolation & purification</subject><subject>Bacteriology</subject><subject>Biomedical and Life Sciences</subject><subject>Bioorganic Chemistry</subject><subject>Chromatography, Affinity</subject><subject>DNA, Bacterial - genetics</subject><subject>Gene Expression Regulation, Bacterial</subject><subject>Life Sciences</subject><subject>Medicinal Chemistry</subject><subject>Metabolites</subject><subject>Microbiology</subject><subject>Mutagenesis, Insertional</subject><subject>Mutation</subject><subject>Organic Chemistry</subject><subject>original-article</subject><subject>Phosphoproteins - chemistry</subject><subject>Phosphoproteins - metabolism</subject><subject>Proteins</subject><subject>S-Adenosylmethionine - pharmacology</subject><subject>Streptomyces coelicolor - drug effects</subject><subject>Streptomyces coelicolor - genetics</subject><subject>Streptomyces coelicolor - metabolism</subject><subject>Tandem Mass Spectrometry</subject><issn>0021-8820</issn><issn>1881-1469</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNptkU2LFDEQhoMo7rh68i4NHjxo1nx0OumjLH4sDLiweg6ZdMXJ0J20SXph_o8_1DQzisiekqKePFXkReglJVeUcPX-YK4YWYtWPUIbqhTFtO36x2hDCKNYKUYu0LOcD4RwyaV6ii4YpbzvGN-gX7f7mOd9nFMs4ENjnPPBl2MzL8k7b03xMTR-gFBqCbk5g7nx4T6O9zDUS3OHTSViPo54iyco-_rIB8A-DIutCIS9CRamammia0yV7Xws3q66ipyGVE9JMJc4HW2dZCOM3sYxpufoiTNjhhfn8xJ9__Tx2_UXvP36-eb6wxbblvYFS-nannDS9UAVdUJK5qQwjgtKhDDQOVa_wDABynSK29ZQZ3Zd1xojQAw9v0RvTt661c8FctGTzxbG0QSIS9aqVZx2TIlKvv6PPMQlhbqcplJJIRnrV9_bE2VTzDmB03Pyk0lHTYles9MHo9fsdM2u0q_OzmU3wfCX_RNWBd6dgFxb4Qekf4Y-4PsNgP-nFw</recordid><startdate>20110101</startdate><enddate>20110101</enddate><creator>Meng, Lingzhu</creator><creator>Yang, Seung Hwan</creator><creator>Palaniyandi, Sasikumar Arunachalam</creator><creator>Lee, Sung-Kwon</creator><creator>Lee, In-Ae</creator><creator>Kim, Tae-Jong</creator><creator>Suh, Joo-Won</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</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>3V.</scope><scope>7QL</scope><scope>7T5</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20110101</creationdate><title>Phosphoprotein affinity purification identifies proteins involved in S-adenosyl-L-methionine-induced enhancement of antibiotic production in Streptomyces coelicolor</title><author>Meng, Lingzhu ; Yang, Seung Hwan ; Palaniyandi, Sasikumar Arunachalam ; Lee, Sung-Kwon ; Lee, In-Ae ; Kim, Tae-Jong ; Suh, Joo-Won</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c419t-77f4903069e181f5772f75af351055ae6f2003a25e8a683c4a1fab664aa5e5d93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>631/208/737</topic><topic>631/326/22/1290</topic><topic>631/80/86</topic><topic>631/92/60</topic><topic>Anti-Bacterial Agents - biosynthesis</topic><topic>Antibiotics</topic><topic>Bacterial Proteins - biosynthesis</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - isolation & purification</topic><topic>Bacteriology</topic><topic>Biomedical and Life Sciences</topic><topic>Bioorganic Chemistry</topic><topic>Chromatography, Affinity</topic><topic>DNA, Bacterial - genetics</topic><topic>Gene Expression Regulation, Bacterial</topic><topic>Life Sciences</topic><topic>Medicinal Chemistry</topic><topic>Metabolites</topic><topic>Microbiology</topic><topic>Mutagenesis, Insertional</topic><topic>Mutation</topic><topic>Organic Chemistry</topic><topic>original-article</topic><topic>Phosphoproteins - chemistry</topic><topic>Phosphoproteins - metabolism</topic><topic>Proteins</topic><topic>S-Adenosylmethionine - pharmacology</topic><topic>Streptomyces coelicolor - drug effects</topic><topic>Streptomyces coelicolor - genetics</topic><topic>Streptomyces coelicolor - metabolism</topic><topic>Tandem Mass Spectrometry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Meng, Lingzhu</creatorcontrib><creatorcontrib>Yang, Seung Hwan</creatorcontrib><creatorcontrib>Palaniyandi, Sasikumar Arunachalam</creatorcontrib><creatorcontrib>Lee, Sung-Kwon</creatorcontrib><creatorcontrib>Lee, In-Ae</creatorcontrib><creatorcontrib>Kim, Tae-Jong</creatorcontrib><creatorcontrib>Suh, Joo-Won</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Immunology Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of antibiotics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Meng, Lingzhu</au><au>Yang, Seung Hwan</au><au>Palaniyandi, Sasikumar Arunachalam</au><au>Lee, Sung-Kwon</au><au>Lee, In-Ae</au><au>Kim, Tae-Jong</au><au>Suh, Joo-Won</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphoprotein affinity purification identifies proteins involved in S-adenosyl-L-methionine-induced enhancement of antibiotic production in Streptomyces coelicolor</atitle><jtitle>Journal of antibiotics</jtitle><stitle>J Antibiot</stitle><addtitle>J Antibiot (Tokyo)</addtitle><date>2011-01-01</date><risdate>2011</risdate><volume>64</volume><issue>1</issue><spage>97</spage><epage>101</epage><pages>97-101</pages><issn>0021-8820</issn><eissn>1881-1469</eissn><abstract>Streptomycetes are the major natural source of clinical antibiotics. The enhanced secondary metabolite production of many streptomycetes by
S
-adenosylmethionine (SAM) in previous studies suggested the existence of a common SAM regulatory effect. We screened nine proteins using the phosphoprotein purification column from
Streptomyces coelicolor
. Among them, genes (SCO5477, SCO5113, SCO4647, SCO4885 and SCO1793) for five proteins were disrupted by insertion mutation. The undecylprodigiosin and actinorhodin productions were changed in all mutations. The SAM-induced enhancement of actinorhodin production was abolished by all mutations except SCO4885 mutation, which reduced the production of actinorhodin and undecylprodigiosin with SAM treatment. This study demonstrates that phosphoprotein affinity purification can be used as a screening method to identify the proteins involved SAM signaling.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>21139623</pmid><doi>10.1038/ja.2010.148</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Journal of antibiotics, 2011-01, Vol.64 (1), p.97-101 |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | 631/208/737 631/326/22/1290 631/80/86 631/92/60 Anti-Bacterial Agents - biosynthesis Antibiotics Bacterial Proteins - biosynthesis Bacterial Proteins - genetics Bacterial Proteins - isolation & purification Bacteriology Biomedical and Life Sciences Bioorganic Chemistry Chromatography, Affinity DNA, Bacterial - genetics Gene Expression Regulation, Bacterial Life Sciences Medicinal Chemistry Metabolites Microbiology Mutagenesis, Insertional Mutation Organic Chemistry original-article Phosphoproteins - chemistry Phosphoproteins - metabolism Proteins S-Adenosylmethionine - pharmacology Streptomyces coelicolor - drug effects Streptomyces coelicolor - genetics Streptomyces coelicolor - metabolism Tandem Mass Spectrometry |
| title | Phosphoprotein affinity purification identifies proteins involved in S-adenosyl-L-methionine-induced enhancement of antibiotic production in Streptomyces coelicolor |
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