Oligomerization of the Response Regulator ComE from Streptococcus mutans Is Affected by Phosphorylation
We have previously characterized the interactions of the response regulator ComE from Streptococcus mutans and DNA binding sites through DNase I footprinting and electrophoretic mobility shift assay analysis. Since response regulator functions are often affected by their phosphorylation state, we in...
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| Veröffentlicht in: | Journal of Bacteriology 2012-03, Vol.194 (5), p.1127-1135 |
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| container_title | Journal of Bacteriology |
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| creator | Hung, David C. I Downey, Jennifer S Kreth, Jens Qi, Fengxia Shi, Wenyuan Cvitkovitch, Dennis G Goodman, Steven D |
| description | We have previously characterized the interactions of the response regulator ComE from Streptococcus mutans and DNA binding sites through DNase I footprinting and electrophoretic mobility shift assay analysis. Since response regulator functions are often affected by their phosphorylation state, we investigated how phosphorylation affects the biochemical function of ComE. Unlike many response regulators, we found that the phosphorylation state of ComE does not likely play a role in DNA binding affinity but rather seems to induce the formation of an oligomeric form of the protein. The role of this oligomerization state for ComE function is discussed. |
| doi_str_mv | 10.1128/JB.06565-11 |
| format | Article |
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I ; Downey, Jennifer S ; Kreth, Jens ; Qi, Fengxia ; Shi, Wenyuan ; Cvitkovitch, Dennis G ; Goodman, Steven D</creator><creatorcontrib>Hung, David C. I ; Downey, Jennifer S ; Kreth, Jens ; Qi, Fengxia ; Shi, Wenyuan ; Cvitkovitch, Dennis G ; Goodman, Steven D</creatorcontrib><description>We have previously characterized the interactions of the response regulator ComE from Streptococcus mutans and DNA binding sites through DNase I footprinting and electrophoretic mobility shift assay analysis. Since response regulator functions are often affected by their phosphorylation state, we investigated how phosphorylation affects the biochemical function of ComE. Unlike many response regulators, we found that the phosphorylation state of ComE does not likely play a role in DNA binding affinity but rather seems to induce the formation of an oligomeric form of the protein. The role of this oligomerization state for ComE function is discussed.</description><identifier>ISSN: 0021-9193</identifier><identifier>EISSN: 1098-5530</identifier><identifier>EISSN: 1067-8832</identifier><identifier>DOI: 10.1128/JB.06565-11</identifier><identifier>PMID: 22210762</identifier><identifier>CODEN: JOBAAY</identifier><language>eng</language><publisher>Washington, DC: American Society for Microbiology</publisher><subject>Bacterial Proteins - metabolism ; Bacteriology ; binding capacity ; Binding sites ; Biological and medical sciences ; deoxyribonuclease I ; Deoxyribonucleic acid ; DNA ; DNA, Bacterial - metabolism ; DNA-Binding Proteins - metabolism ; Fundamental and applied biological sciences. Psychology ; gel electrophoresis ; Microbiology ; Miscellaneous ; Phosphorylation ; Protein Binding ; Protein Multimerization ; Proteins ; Streptococcus infections ; Streptococcus mutans ; Streptococcus mutans - metabolism</subject><ispartof>Journal of Bacteriology, 2012-03, Vol.194 (5), p.1127-1135</ispartof><rights>2015 INIST-CNRS</rights><rights>Copyright American Society for Microbiology Mar 2012</rights><rights>Copyright © 2012, American Society for Microbiology. All Rights Reserved. 2012 American Society for Microbiology</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c520t-5f6ebcea610ba6de3cb08f6cb0dd589171486f6689cc3200c5223d32db5f68193</citedby><cites>FETCH-LOGICAL-c520t-5f6ebcea610ba6de3cb08f6cb0dd589171486f6689cc3200c5223d32db5f68193</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/PMC3294772/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3294772/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27903,27904,53769,53771</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=25543631$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22210762$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hung, David C. I</creatorcontrib><creatorcontrib>Downey, Jennifer S</creatorcontrib><creatorcontrib>Kreth, Jens</creatorcontrib><creatorcontrib>Qi, Fengxia</creatorcontrib><creatorcontrib>Shi, Wenyuan</creatorcontrib><creatorcontrib>Cvitkovitch, Dennis G</creatorcontrib><creatorcontrib>Goodman, Steven D</creatorcontrib><title>Oligomerization of the Response Regulator ComE from Streptococcus mutans Is Affected by Phosphorylation</title><title>Journal of Bacteriology</title><addtitle>J Bacteriol</addtitle><description>We have previously characterized the interactions of the response regulator ComE from Streptococcus mutans and DNA binding sites through DNase I footprinting and electrophoretic mobility shift assay analysis. Since response regulator functions are often affected by their phosphorylation state, we investigated how phosphorylation affects the biochemical function of ComE. Unlike many response regulators, we found that the phosphorylation state of ComE does not likely play a role in DNA binding affinity but rather seems to induce the formation of an oligomeric form of the protein. The role of this oligomerization state for ComE function is discussed.</description><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriology</subject><subject>binding capacity</subject><subject>Binding sites</subject><subject>Biological and medical sciences</subject><subject>deoxyribonuclease I</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA, Bacterial - metabolism</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>gel electrophoresis</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>Phosphorylation</subject><subject>Protein Binding</subject><subject>Protein Multimerization</subject><subject>Proteins</subject><subject>Streptococcus infections</subject><subject>Streptococcus mutans</subject><subject>Streptococcus mutans - metabolism</subject><issn>0021-9193</issn><issn>1098-5530</issn><issn>1067-8832</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kktv1DAQgCMEokvhxB1cJAQSSrHHsRNfkNpVgVaViig9W45jJ1klcbAT0PLrcbpLeRy4-CF_843H4yR5SvAxIVC8vTg9xpxxlhJyL1kRLIqUMYrvJyuMgaSCCHqQPAphgzHJMgYPkwMAIDjnsErqq66tXW98-0NNrRuQs2hqDPpswuiGsCzquVOT82jt-jNkvevR9eTNODnttJ4D6udJDQGdB3RirdGTqVC5RZ8aF8bG-W13632cPLCqC-bJfj5Mbt6ffVl_TC-vPpyvTy5TzQBPKbPclNooTnCpeGWoLnFheRyrihWC5CQruOW8EFpTwDhGAa0oVGWMLGKlh8m7nXecy95U2gyTV50cfdsrv5VOtfLvk6FtZO2-SQoiy3OIgld7gXdfZxMm2bdBm65Tg3FzkAJIBoyTIpKv_0sSnhcMijznEX3xD7pxsx_iQ0Qf5NEJNEJvdpD2LgRv7N2tCZZLp-XFqbztdNxF-tmfhd6xv1obgZd7QAWtOuvVoNvwm2Mso5wuoqMd17R18731RqrQy00picjkkgryyDzfMVY5qWofPTfXgAlbvpQQIOhPMGDFfg</recordid><startdate>20120301</startdate><enddate>20120301</enddate><creator>Hung, David C. 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I ; Downey, Jennifer S ; Kreth, Jens ; Qi, Fengxia ; Shi, Wenyuan ; Cvitkovitch, Dennis G ; Goodman, Steven D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c520t-5f6ebcea610ba6de3cb08f6cb0dd589171486f6689cc3200c5223d32db5f68193</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Bacterial Proteins - metabolism</topic><topic>Bacteriology</topic><topic>binding capacity</topic><topic>Binding sites</topic><topic>Biological and medical sciences</topic><topic>deoxyribonuclease I</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>DNA, Bacterial - metabolism</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>gel electrophoresis</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>Phosphorylation</topic><topic>Protein Binding</topic><topic>Protein Multimerization</topic><topic>Proteins</topic><topic>Streptococcus infections</topic><topic>Streptococcus mutans</topic><topic>Streptococcus mutans - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hung, David C. 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I</au><au>Downey, Jennifer S</au><au>Kreth, Jens</au><au>Qi, Fengxia</au><au>Shi, Wenyuan</au><au>Cvitkovitch, Dennis G</au><au>Goodman, Steven D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Oligomerization of the Response Regulator ComE from Streptococcus mutans Is Affected by Phosphorylation</atitle><jtitle>Journal of Bacteriology</jtitle><addtitle>J Bacteriol</addtitle><date>2012-03-01</date><risdate>2012</risdate><volume>194</volume><issue>5</issue><spage>1127</spage><epage>1135</epage><pages>1127-1135</pages><issn>0021-9193</issn><eissn>1098-5530</eissn><eissn>1067-8832</eissn><coden>JOBAAY</coden><abstract>We have previously characterized the interactions of the response regulator ComE from Streptococcus mutans and DNA binding sites through DNase I footprinting and electrophoretic mobility shift assay analysis. 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| subjects | Bacterial Proteins - metabolism Bacteriology binding capacity Binding sites Biological and medical sciences deoxyribonuclease I Deoxyribonucleic acid DNA DNA, Bacterial - metabolism DNA-Binding Proteins - metabolism Fundamental and applied biological sciences. Psychology gel electrophoresis Microbiology Miscellaneous Phosphorylation Protein Binding Protein Multimerization Proteins Streptococcus infections Streptococcus mutans Streptococcus mutans - metabolism |
| title | Oligomerization of the Response Regulator ComE from Streptococcus mutans Is Affected by Phosphorylation |
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