Kinetics of CheY phosphorylation by small molecule phosphodonors
The chemotaxis response regulator CheY can acquire phosphoryl groups either from its associated autophosphorylating protein kinase, CheA, or from small phosphodonor molecules such as acetyl phosphate. We report a stopped-flow kinetic analysis of CheY phosphorylation by acetyl phosphate. The results...
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Veröffentlicht in: | FEBS letters 1999-09, Vol.457 (3), p.323-326 |
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creator | Da Re, Sandra S. Deville-Bonne, Dominique Tolstykh, Tatiana Véron, Michel Stock, Jeffry B. |
description | The chemotaxis response regulator CheY can acquire phosphoryl groups either from its associated autophosphorylating protein kinase, CheA, or from small phosphodonor molecules such as acetyl phosphate. We report a stopped-flow kinetic analysis of CheY phosphorylation by acetyl phosphate. The results show that CheY has a very low affinity for this phosphodonor (
K
s≫0.1 M), consistent with the conclusion that, whereas CheY provides catalytic functions for the phosphotransfer reaction, the CheA kinase may act simply to increase the effective phosphodonor concentration at the CheY active site. |
doi_str_mv | 10.1016/S0014-5793(99)01057-1 |
format | Article |
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K
s≫0.1 M), consistent with the conclusion that, whereas CheY provides catalytic functions for the phosphotransfer reaction, the CheA kinase may act simply to increase the effective phosphodonor concentration at the CheY active site.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(99)01057-1</identifier><identifier>PMID: 10471801</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>AcP, acetyl phosphate ; Amides - chemistry ; Amides - metabolism ; Bacterial Proteins ; Biochemistry - instrumentation ; Biochemistry - methods ; Chemotaxis ; Fluorescence ; Histidine - analogs & derivatives ; Histidine - metabolism ; HPK, histidine protein kinase ; Kinetics ; Membrane Proteins - chemistry ; Membrane Proteins - metabolism ; Methyl-Accepting Chemotaxis Proteins ; Organophosphates - chemistry ; Organophosphates - metabolism ; Pam, Phosphoramidate ; Phosphoric Acids - chemistry ; Phosphoric Acids - metabolism ; Phosphorylation ; Phosphotransfer ; Two-component system</subject><ispartof>FEBS letters, 1999-09, Vol.457 (3), p.323-326</ispartof><rights>1999 Federation of European Biochemical Societies</rights><rights>FEBS Letters 457 (1999) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4781-5d3b0b58f299634efe940bc573e14776b715ec07f1719b3e8ed039ed99ab18623</citedby><cites>FETCH-LOGICAL-c4781-5d3b0b58f299634efe940bc573e14776b715ec07f1719b3e8ed039ed99ab18623</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%2FS0014-5793%2899%2901057-1$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0014-5793(99)01057-1$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,1417,1433,3550,27924,27925,45574,45575,45995,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10471801$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Da Re, Sandra S.</creatorcontrib><creatorcontrib>Deville-Bonne, Dominique</creatorcontrib><creatorcontrib>Tolstykh, Tatiana</creatorcontrib><creatorcontrib>Véron, Michel</creatorcontrib><creatorcontrib>Stock, Jeffry B.</creatorcontrib><title>Kinetics of CheY phosphorylation by small molecule phosphodonors</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>The chemotaxis response regulator CheY can acquire phosphoryl groups either from its associated autophosphorylating protein kinase, CheA, or from small phosphodonor molecules such as acetyl phosphate. We report a stopped-flow kinetic analysis of CheY phosphorylation by acetyl phosphate. The results show that CheY has a very low affinity for this phosphodonor (
K
s≫0.1 M), consistent with the conclusion that, whereas CheY provides catalytic functions for the phosphotransfer reaction, the CheA kinase may act simply to increase the effective phosphodonor concentration at the CheY active site.</description><subject>AcP, acetyl phosphate</subject><subject>Amides - chemistry</subject><subject>Amides - metabolism</subject><subject>Bacterial Proteins</subject><subject>Biochemistry - instrumentation</subject><subject>Biochemistry - methods</subject><subject>Chemotaxis</subject><subject>Fluorescence</subject><subject>Histidine - analogs & derivatives</subject><subject>Histidine - metabolism</subject><subject>HPK, histidine protein kinase</subject><subject>Kinetics</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - metabolism</subject><subject>Methyl-Accepting Chemotaxis Proteins</subject><subject>Organophosphates - chemistry</subject><subject>Organophosphates - metabolism</subject><subject>Pam, Phosphoramidate</subject><subject>Phosphoric Acids - chemistry</subject><subject>Phosphoric Acids - metabolism</subject><subject>Phosphorylation</subject><subject>Phosphotransfer</subject><subject>Two-component system</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkD1PwzAQhi0EoqXwE0CZEAwBX53E8cRH1VJEJQZgYLIS56IaOXGxU1D_PWlTEBsMlmXfc-_ZDyHHQC-AQnL5RClEYcwFOxPinAKNeQg7pA8pZyGLknSX9H-QHjnw_o225xTEPukBjTikFPrk-kHX2GjlA1sGozm-Bou59e1yK5M12tZBvgp8lRkTVNagWhr8JgpbW-cPyV6ZGY9H231AXibj59E0nD3e3Y9uZqGKeAphXLCc5nFaDoVIWIQliojmKuYMIeI8yTnEqCgvgYPIGaZYUCawECLLIU2GbEBOu9yFs-9L9I2stFdoTFajXXrJ29-JYUxbMO5A5az3Dku5cLrK3EoClWt1cqNOrr1IIeRGnYS272Q7YJlXWPzq6ly1wLQDPrXB1f9S5WR8O9xU1gUhNtfrqKsuCltjHxqd9EpjrbDQDlUjC6v_eO0XVk6RVQ</recordid><startdate>19990903</startdate><enddate>19990903</enddate><creator>Da Re, Sandra S.</creator><creator>Deville-Bonne, Dominique</creator><creator>Tolstykh, Tatiana</creator><creator>Véron, Michel</creator><creator>Stock, Jeffry B.</creator><general>Elsevier B.V</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>7X8</scope></search><sort><creationdate>19990903</creationdate><title>Kinetics of CheY phosphorylation by small molecule phosphodonors</title><author>Da Re, Sandra S. ; Deville-Bonne, Dominique ; Tolstykh, Tatiana ; Véron, Michel ; Stock, Jeffry B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4781-5d3b0b58f299634efe940bc573e14776b715ec07f1719b3e8ed039ed99ab18623</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>AcP, acetyl phosphate</topic><topic>Amides - chemistry</topic><topic>Amides - metabolism</topic><topic>Bacterial Proteins</topic><topic>Biochemistry - instrumentation</topic><topic>Biochemistry - methods</topic><topic>Chemotaxis</topic><topic>Fluorescence</topic><topic>Histidine - analogs & derivatives</topic><topic>Histidine - metabolism</topic><topic>HPK, histidine protein kinase</topic><topic>Kinetics</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - metabolism</topic><topic>Methyl-Accepting Chemotaxis Proteins</topic><topic>Organophosphates - chemistry</topic><topic>Organophosphates - metabolism</topic><topic>Pam, Phosphoramidate</topic><topic>Phosphoric Acids - chemistry</topic><topic>Phosphoric Acids - metabolism</topic><topic>Phosphorylation</topic><topic>Phosphotransfer</topic><topic>Two-component system</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Da Re, Sandra S.</creatorcontrib><creatorcontrib>Deville-Bonne, Dominique</creatorcontrib><creatorcontrib>Tolstykh, Tatiana</creatorcontrib><creatorcontrib>Véron, Michel</creatorcontrib><creatorcontrib>Stock, Jeffry B.</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>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Da Re, Sandra S.</au><au>Deville-Bonne, Dominique</au><au>Tolstykh, Tatiana</au><au>Véron, Michel</au><au>Stock, Jeffry B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Kinetics of CheY phosphorylation by small molecule phosphodonors</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1999-09-03</date><risdate>1999</risdate><volume>457</volume><issue>3</issue><spage>323</spage><epage>326</epage><pages>323-326</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>The chemotaxis response regulator CheY can acquire phosphoryl groups either from its associated autophosphorylating protein kinase, CheA, or from small phosphodonor molecules such as acetyl phosphate. We report a stopped-flow kinetic analysis of CheY phosphorylation by acetyl phosphate. The results show that CheY has a very low affinity for this phosphodonor (
K
s≫0.1 M), consistent with the conclusion that, whereas CheY provides catalytic functions for the phosphotransfer reaction, the CheA kinase may act simply to increase the effective phosphodonor concentration at the CheY active site.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>10471801</pmid><doi>10.1016/S0014-5793(99)01057-1</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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source | MEDLINE; Wiley Journals; Wiley Online Library Free Content; Access via ScienceDirect (Elsevier); EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
subjects | AcP, acetyl phosphate Amides - chemistry Amides - metabolism Bacterial Proteins Biochemistry - instrumentation Biochemistry - methods Chemotaxis Fluorescence Histidine - analogs & derivatives Histidine - metabolism HPK, histidine protein kinase Kinetics Membrane Proteins - chemistry Membrane Proteins - metabolism Methyl-Accepting Chemotaxis Proteins Organophosphates - chemistry Organophosphates - metabolism Pam, Phosphoramidate Phosphoric Acids - chemistry Phosphoric Acids - metabolism Phosphorylation Phosphotransfer Two-component system |
title | Kinetics of CheY phosphorylation by small molecule phosphodonors |
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