S-Cysteinylation Is a General Mechanism for Thiol Protection of Bacillus subtilis Proteins after Oxidative Stress
S-Thiolation is crucial for protection and regulation of thiol-containing proteins during oxidative stress and is frequently achieved by the formation of mixed disulfides with glutathione. However, many Gram-positive bacteria including Bacillus subtilis lack the low molecular weight (LMW) thiol glut...
Gespeichert in:
| Veröffentlicht in: | The Journal of biological chemistry 2007-09, Vol.282 (36), p.25981-25985 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 25985 |
|---|---|
| container_issue | 36 |
| container_start_page | 25981 |
| container_title | The Journal of biological chemistry |
| container_volume | 282 |
| creator | Hochgräfe, Falko Mostertz, Jörg Pöther, Dierk-Christoph Becher, Dörte Helmann, John D. Hecker, Michael |
| description | S-Thiolation is crucial for protection and regulation of thiol-containing proteins during oxidative stress and is frequently achieved by the formation of mixed disulfides with glutathione. However, many Gram-positive bacteria including Bacillus subtilis lack the low molecular weight (LMW) thiol glutathione. Here we provide evidence that S-thiolation by the LMW thiol cysteine represents a general mechanism in B. subtilis. In vivo labeling of proteins with [35S]cysteine and nonreducing two-dimensional PAGE analyses revealed that a large subset of proteins previously identified as having redox-sensitive thiols are modified by cysteine in response to treatment with the thiol-specific oxidant diamide. By means of multidimensional shotgun proteomics, the sites of S-cysteinylation for six proteins could be identified, three of which are known to be S-glutathionylated in other organisms. |
| doi_str_mv | 10.1074/jbc.C700105200 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_68232451</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0021925820745205</els_id><sourcerecordid>68232451</sourcerecordid><originalsourceid>FETCH-LOGICAL-c487t-eba9deca11d934f11bd55719666f4bae704acd258b0700462680a04bdea583ab3</originalsourceid><addsrcrecordid>eNqFkUFv1DAQhS0EokvLlSPyAXHL4knsxDnCCkqloiK1lbhZtjMhrpK4tZ22--9xyUo9IeYyh_nmad48Qt4B2wJr-KcbY7e7hjFgomTsBdkAk1VRCfj1kmwYK6FoSyGPyJsYb1gu3sJrcgRNDQBttSF3l8VuHxO6eT_q5PxMzyLV9BRnDHqkP9AOenZxor0P9GpwfqQ_g09o_7K-p1-0deO4RBoXk9zo4jp3c5bpEwZ68ei6rHyP9DIFjPGEvOr1GPHtoR-T629fr3bfi_OL07Pd5_PCctmkAo1uO7QaoGsr3gOYTogG2rque240Noxr22VvhmX7vC5ryTTjpkMtZKVNdUw-rrq3wd8tGJOaXLQ4jnpGv0RVy7IquYD_gtByIVkjMrhdQRt8jAF7dRvcpMNeAVNPaaichnpOIy-8PygvZsLuGT-8PwMfVmBwv4cHF1AZ5-2AkyplqapalaKVTxfKFcP8r3uHQUXrcLbY5RWbVOfdv074A6cppRU</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>19458075</pqid></control><display><type>article</type><title>S-Cysteinylation Is a General Mechanism for Thiol Protection of Bacillus subtilis Proteins after Oxidative Stress</title><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><creator>Hochgräfe, Falko ; Mostertz, Jörg ; Pöther, Dierk-Christoph ; Becher, Dörte ; Helmann, John D. ; Hecker, Michael</creator><creatorcontrib>Hochgräfe, Falko ; Mostertz, Jörg ; Pöther, Dierk-Christoph ; Becher, Dörte ; Helmann, John D. ; Hecker, Michael</creatorcontrib><description>S-Thiolation is crucial for protection and regulation of thiol-containing proteins during oxidative stress and is frequently achieved by the formation of mixed disulfides with glutathione. However, many Gram-positive bacteria including Bacillus subtilis lack the low molecular weight (LMW) thiol glutathione. Here we provide evidence that S-thiolation by the LMW thiol cysteine represents a general mechanism in B. subtilis. In vivo labeling of proteins with [35S]cysteine and nonreducing two-dimensional PAGE analyses revealed that a large subset of proteins previously identified as having redox-sensitive thiols are modified by cysteine in response to treatment with the thiol-specific oxidant diamide. By means of multidimensional shotgun proteomics, the sites of S-cysteinylation for six proteins could be identified, three of which are known to be S-glutathionylated in other organisms.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.C700105200</identifier><identifier>PMID: 17611193</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Bacillus subtilis ; Bacillus subtilis - metabolism ; Bacterial Proteins - analysis ; Bacterial Proteins - metabolism ; Cysteine - analysis ; Cysteine - metabolism ; Diamide - analysis ; Diamide - metabolism ; Electrophoresis, Gel, Two-Dimensional ; Glutathione - deficiency ; Glutathione - metabolism ; Oxidative Stress - physiology ; Protein Processing, Post-Translational - physiology</subject><ispartof>The Journal of biological chemistry, 2007-09, Vol.282 (36), p.25981-25985</ispartof><rights>2007 © 2007 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c487t-eba9deca11d934f11bd55719666f4bae704acd258b0700462680a04bdea583ab3</citedby><cites>FETCH-LOGICAL-c487t-eba9deca11d934f11bd55719666f4bae704acd258b0700462680a04bdea583ab3</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/17611193$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hochgräfe, Falko</creatorcontrib><creatorcontrib>Mostertz, Jörg</creatorcontrib><creatorcontrib>Pöther, Dierk-Christoph</creatorcontrib><creatorcontrib>Becher, Dörte</creatorcontrib><creatorcontrib>Helmann, John D.</creatorcontrib><creatorcontrib>Hecker, Michael</creatorcontrib><title>S-Cysteinylation Is a General Mechanism for Thiol Protection of Bacillus subtilis Proteins after Oxidative Stress</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>S-Thiolation is crucial for protection and regulation of thiol-containing proteins during oxidative stress and is frequently achieved by the formation of mixed disulfides with glutathione. However, many Gram-positive bacteria including Bacillus subtilis lack the low molecular weight (LMW) thiol glutathione. Here we provide evidence that S-thiolation by the LMW thiol cysteine represents a general mechanism in B. subtilis. In vivo labeling of proteins with [35S]cysteine and nonreducing two-dimensional PAGE analyses revealed that a large subset of proteins previously identified as having redox-sensitive thiols are modified by cysteine in response to treatment with the thiol-specific oxidant diamide. By means of multidimensional shotgun proteomics, the sites of S-cysteinylation for six proteins could be identified, three of which are known to be S-glutathionylated in other organisms.</description><subject>Bacillus subtilis</subject><subject>Bacillus subtilis - metabolism</subject><subject>Bacterial Proteins - analysis</subject><subject>Bacterial Proteins - metabolism</subject><subject>Cysteine - analysis</subject><subject>Cysteine - metabolism</subject><subject>Diamide - analysis</subject><subject>Diamide - metabolism</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Glutathione - deficiency</subject><subject>Glutathione - metabolism</subject><subject>Oxidative Stress - physiology</subject><subject>Protein Processing, Post-Translational - physiology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFv1DAQhS0EokvLlSPyAXHL4knsxDnCCkqloiK1lbhZtjMhrpK4tZ22--9xyUo9IeYyh_nmad48Qt4B2wJr-KcbY7e7hjFgomTsBdkAk1VRCfj1kmwYK6FoSyGPyJsYb1gu3sJrcgRNDQBttSF3l8VuHxO6eT_q5PxMzyLV9BRnDHqkP9AOenZxor0P9GpwfqQ_g09o_7K-p1-0deO4RBoXk9zo4jp3c5bpEwZ68ei6rHyP9DIFjPGEvOr1GPHtoR-T629fr3bfi_OL07Pd5_PCctmkAo1uO7QaoGsr3gOYTogG2rque240Noxr22VvhmX7vC5ryTTjpkMtZKVNdUw-rrq3wd8tGJOaXLQ4jnpGv0RVy7IquYD_gtByIVkjMrhdQRt8jAF7dRvcpMNeAVNPaaichnpOIy-8PygvZsLuGT-8PwMfVmBwv4cHF1AZ5-2AkyplqapalaKVTxfKFcP8r3uHQUXrcLbY5RWbVOfdv074A6cppRU</recordid><startdate>20070907</startdate><enddate>20070907</enddate><creator>Hochgräfe, Falko</creator><creator>Mostertz, Jörg</creator><creator>Pöther, Dierk-Christoph</creator><creator>Becher, Dörte</creator><creator>Helmann, John D.</creator><creator>Hecker, Michael</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20070907</creationdate><title>S-Cysteinylation Is a General Mechanism for Thiol Protection of Bacillus subtilis Proteins after Oxidative Stress</title><author>Hochgräfe, Falko ; Mostertz, Jörg ; Pöther, Dierk-Christoph ; Becher, Dörte ; Helmann, John D. ; Hecker, Michael</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c487t-eba9deca11d934f11bd55719666f4bae704acd258b0700462680a04bdea583ab3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Bacillus subtilis</topic><topic>Bacillus subtilis - metabolism</topic><topic>Bacterial Proteins - analysis</topic><topic>Bacterial Proteins - metabolism</topic><topic>Cysteine - analysis</topic><topic>Cysteine - metabolism</topic><topic>Diamide - analysis</topic><topic>Diamide - metabolism</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Glutathione - deficiency</topic><topic>Glutathione - metabolism</topic><topic>Oxidative Stress - physiology</topic><topic>Protein Processing, Post-Translational - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hochgräfe, Falko</creatorcontrib><creatorcontrib>Mostertz, Jörg</creatorcontrib><creatorcontrib>Pöther, Dierk-Christoph</creatorcontrib><creatorcontrib>Becher, Dörte</creatorcontrib><creatorcontrib>Helmann, John D.</creatorcontrib><creatorcontrib>Hecker, Michael</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hochgräfe, Falko</au><au>Mostertz, Jörg</au><au>Pöther, Dierk-Christoph</au><au>Becher, Dörte</au><au>Helmann, John D.</au><au>Hecker, Michael</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>S-Cysteinylation Is a General Mechanism for Thiol Protection of Bacillus subtilis Proteins after Oxidative Stress</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2007-09-07</date><risdate>2007</risdate><volume>282</volume><issue>36</issue><spage>25981</spage><epage>25985</epage><pages>25981-25985</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>S-Thiolation is crucial for protection and regulation of thiol-containing proteins during oxidative stress and is frequently achieved by the formation of mixed disulfides with glutathione. However, many Gram-positive bacteria including Bacillus subtilis lack the low molecular weight (LMW) thiol glutathione. Here we provide evidence that S-thiolation by the LMW thiol cysteine represents a general mechanism in B. subtilis. In vivo labeling of proteins with [35S]cysteine and nonreducing two-dimensional PAGE analyses revealed that a large subset of proteins previously identified as having redox-sensitive thiols are modified by cysteine in response to treatment with the thiol-specific oxidant diamide. By means of multidimensional shotgun proteomics, the sites of S-cysteinylation for six proteins could be identified, three of which are known to be S-glutathionylated in other organisms.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>17611193</pmid><doi>10.1074/jbc.C700105200</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 2007-09, Vol.282 (36), p.25981-25985 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_68232451 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Bacillus subtilis Bacillus subtilis - metabolism Bacterial Proteins - analysis Bacterial Proteins - metabolism Cysteine - analysis Cysteine - metabolism Diamide - analysis Diamide - metabolism Electrophoresis, Gel, Two-Dimensional Glutathione - deficiency Glutathione - metabolism Oxidative Stress - physiology Protein Processing, Post-Translational - physiology |
| title | S-Cysteinylation Is a General Mechanism for Thiol Protection of Bacillus subtilis Proteins after Oxidative Stress |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-23T17%3A54%3A35IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=S-Cysteinylation%20Is%20a%20General%20Mechanism%20for%20Thiol%20Protection%20of%20Bacillus%20subtilis%20Proteins%20after%20Oxidative%20Stress&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Hochgr%C3%A4fe,%20Falko&rft.date=2007-09-07&rft.volume=282&rft.issue=36&rft.spage=25981&rft.epage=25985&rft.pages=25981-25985&rft.issn=0021-9258&rft.eissn=1083-351X&rft_id=info:doi/10.1074/jbc.C700105200&rft_dat=%3Cproquest_cross%3E68232451%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=19458075&rft_id=info:pmid/17611193&rft_els_id=S0021925820745205&rfr_iscdi=true |