Investigation of transphosphorylation between chemotaxis proteins and the phosphoenolpyruvate: sugar phosphotransferase system
Transphosphorylation between the chemotaxis proteins and phosphoenolpyruvate:sugar phosphotransferase system (PTS) from Escherichia coli was investigated by incubating the CheA, CheW and CheY proteins of the chemotaxis cascade, and Enzyme I, HPr and Enzyme II mtl of the PTS with [γ- 32P]ATP or [ 32P...
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| Veröffentlicht in: | FEBS letters 1995-10, Vol.374 (2), p.161-164 |
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| creator | Johnson, Mark S. Rowsell, Edward H. Taylor, Barry L. |
| description | Transphosphorylation between the chemotaxis proteins and phosphoenolpyruvate:sugar phosphotransferase system (PTS) from
Escherichia coli was investigated by incubating the CheA, CheW and CheY proteins of the chemotaxis cascade, and Enzyme I, HPr and Enzyme II
mtl of the PTS with [γ-
32P]ATP or [
32P]phosphoenolpyruvate in the presence and absence of cell extract. In the absence of cell extract, ATP phosphorylated CheA, but in the presence of cell extract, Enzyme I was also phosphorylated. Phosphoenolpyruvate phosphorylated only PTS components. The transphosphorylation of Enzyme I by ATP did not require chemotaxis proteins, and likely occurred through acetate kinase. Regardless of phosphorylation state, the HPr protein did not inhibit the rate of ATP-dependent phosphorylation of the CheA or the CheY protein. It is concluded that chemotaxis to PTS substrates is not mediated by transphosphorylation between the PTS and chemotaxis systems. |
| doi_str_mv | 10.1016/0014-5793(95)01097-X |
| format | Article |
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Escherichia coli was investigated by incubating the CheA, CheW and CheY proteins of the chemotaxis cascade, and Enzyme I, HPr and Enzyme II
mtl of the PTS with [γ-
32P]ATP or [
32P]phosphoenolpyruvate in the presence and absence of cell extract. In the absence of cell extract, ATP phosphorylated CheA, but in the presence of cell extract, Enzyme I was also phosphorylated. Phosphoenolpyruvate phosphorylated only PTS components. The transphosphorylation of Enzyme I by ATP did not require chemotaxis proteins, and likely occurred through acetate kinase. Regardless of phosphorylation state, the HPr protein did not inhibit the rate of ATP-dependent phosphorylation of the CheA or the CheY protein. It is concluded that chemotaxis to PTS substrates is not mediated by transphosphorylation between the PTS and chemotaxis systems.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(95)01097-X</identifier><identifier>PMID: 7589525</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Acetate kinase ; Bacterial chemotaxis ; Bacterial Proteins - metabolism ; CheA protein ; Chemotaxis ; CheY protein ; Enzyme I ; Escherichia coli ; Escherichia coli - enzymology ; Escherichia coli - physiology ; Escherichia coli Proteins ; Histidine Kinase ; Membrane Proteins - metabolism ; Methyl-Accepting Chemotaxis Proteins ; Phosphoenolpyruvate Sugar Phosphotransferase System - metabolism ; Phosphorylation ; Phosphotransferase system ; Salmonella typhimurium - enzymology ; Salmonella typhimurium - physiology</subject><ispartof>FEBS letters, 1995-10, Vol.374 (2), p.161-164</ispartof><rights>1995</rights><rights>FEBS Letters 374 (1995) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c497X-f6a671a07011304dd61a08c214e7a322f9a7cf4ce97fddd9ed49772ad65eaee83</citedby><cites>FETCH-LOGICAL-c497X-f6a671a07011304dd61a08c214e7a322f9a7cf4ce97fddd9ed49772ad65eaee83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/001457939501097X$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7589525$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Johnson, Mark S.</creatorcontrib><creatorcontrib>Rowsell, Edward H.</creatorcontrib><creatorcontrib>Taylor, Barry L.</creatorcontrib><title>Investigation of transphosphorylation between chemotaxis proteins and the phosphoenolpyruvate: sugar phosphotransferase system</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Transphosphorylation between the chemotaxis proteins and phosphoenolpyruvate:sugar phosphotransferase system (PTS) from
Escherichia coli was investigated by incubating the CheA, CheW and CheY proteins of the chemotaxis cascade, and Enzyme I, HPr and Enzyme II
mtl of the PTS with [γ-
32P]ATP or [
32P]phosphoenolpyruvate in the presence and absence of cell extract. In the absence of cell extract, ATP phosphorylated CheA, but in the presence of cell extract, Enzyme I was also phosphorylated. Phosphoenolpyruvate phosphorylated only PTS components. The transphosphorylation of Enzyme I by ATP did not require chemotaxis proteins, and likely occurred through acetate kinase. Regardless of phosphorylation state, the HPr protein did not inhibit the rate of ATP-dependent phosphorylation of the CheA or the CheY protein. It is concluded that chemotaxis to PTS substrates is not mediated by transphosphorylation between the PTS and chemotaxis systems.</description><subject>Acetate kinase</subject><subject>Bacterial chemotaxis</subject><subject>Bacterial Proteins - metabolism</subject><subject>CheA protein</subject><subject>Chemotaxis</subject><subject>CheY protein</subject><subject>Enzyme I</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - physiology</subject><subject>Escherichia coli Proteins</subject><subject>Histidine Kinase</subject><subject>Membrane Proteins - metabolism</subject><subject>Methyl-Accepting Chemotaxis Proteins</subject><subject>Phosphoenolpyruvate Sugar Phosphotransferase System - metabolism</subject><subject>Phosphorylation</subject><subject>Phosphotransferase system</subject><subject>Salmonella typhimurium - enzymology</subject><subject>Salmonella typhimurium - physiology</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNUc1u1DAQthCoLKVvAJJPqBwCdhLHNgckqLpQqRIXKu3Ncu1J1yhxFtvZNheeHWez9AgcLGu-P49nEHpFyTtKaPOeEFoXjMvqXLK3hBLJi80TtKKCV0VVN-IpWj1KnqMXMf4guRZUnqATzoRkJVuhX1d-DzG5O53c4PHQ4hS0j7vtMJ8wdQt-C-kewGOzhX5I-sFFvAtDAucj1t7itAV89IAfut0Uxr1O8AHH8U6HP9QhuoWgI-A4xQT9S_Ss1V2Es-N9im7Wl98vvhbX375cXXy6Lkwt-aZoG91wqgknlFaktrbJhTAlrYHrqixbqblpawOSt9ZaCTbbeKltw0ADiOoUvVlyc9c_x_xh1btooOu0h2GMivOGcUbqfwopE40QJcnCehGaMMQYoFW74HodJkWJmvej5uGrefhKMnXYj9pk2-tj_njbg300HReS-fXC37sOpv_KVOvLz-VMzLhkB3R-6OMSBHmsewdBRePAG7AugEnKDu7vnf4G3t24PQ</recordid><startdate>19951030</startdate><enddate>19951030</enddate><creator>Johnson, Mark S.</creator><creator>Rowsell, Edward H.</creator><creator>Taylor, Barry L.</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>7QL</scope><scope>7QR</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19951030</creationdate><title>Investigation of transphosphorylation between chemotaxis proteins and the phosphoenolpyruvate: sugar phosphotransferase system</title><author>Johnson, Mark S. ; Rowsell, Edward H. ; Taylor, Barry L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c497X-f6a671a07011304dd61a08c214e7a322f9a7cf4ce97fddd9ed49772ad65eaee83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Acetate kinase</topic><topic>Bacterial chemotaxis</topic><topic>Bacterial Proteins - metabolism</topic><topic>CheA protein</topic><topic>Chemotaxis</topic><topic>CheY protein</topic><topic>Enzyme I</topic><topic>Escherichia coli</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - physiology</topic><topic>Escherichia coli Proteins</topic><topic>Histidine Kinase</topic><topic>Membrane Proteins - metabolism</topic><topic>Methyl-Accepting Chemotaxis Proteins</topic><topic>Phosphoenolpyruvate Sugar Phosphotransferase System - metabolism</topic><topic>Phosphorylation</topic><topic>Phosphotransferase system</topic><topic>Salmonella typhimurium - enzymology</topic><topic>Salmonella typhimurium - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Johnson, Mark S.</creatorcontrib><creatorcontrib>Rowsell, Edward H.</creatorcontrib><creatorcontrib>Taylor, Barry L.</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>Chemoreception Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Johnson, Mark S.</au><au>Rowsell, Edward H.</au><au>Taylor, Barry L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Investigation of transphosphorylation between chemotaxis proteins and the phosphoenolpyruvate: sugar phosphotransferase system</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1995-10-30</date><risdate>1995</risdate><volume>374</volume><issue>2</issue><spage>161</spage><epage>164</epage><pages>161-164</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Transphosphorylation between the chemotaxis proteins and phosphoenolpyruvate:sugar phosphotransferase system (PTS) from
Escherichia coli was investigated by incubating the CheA, CheW and CheY proteins of the chemotaxis cascade, and Enzyme I, HPr and Enzyme II
mtl of the PTS with [γ-
32P]ATP or [
32P]phosphoenolpyruvate in the presence and absence of cell extract. In the absence of cell extract, ATP phosphorylated CheA, but in the presence of cell extract, Enzyme I was also phosphorylated. Phosphoenolpyruvate phosphorylated only PTS components. The transphosphorylation of Enzyme I by ATP did not require chemotaxis proteins, and likely occurred through acetate kinase. Regardless of phosphorylation state, the HPr protein did not inhibit the rate of ATP-dependent phosphorylation of the CheA or the CheY protein. It is concluded that chemotaxis to PTS substrates is not mediated by transphosphorylation between the PTS and chemotaxis systems.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>7589525</pmid><doi>10.1016/0014-5793(95)01097-X</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | FEBS letters, 1995-10, Vol.374 (2), p.161-164 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77657504 |
| source | MEDLINE; Elsevier ScienceDirect Journals; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Acetate kinase Bacterial chemotaxis Bacterial Proteins - metabolism CheA protein Chemotaxis CheY protein Enzyme I Escherichia coli Escherichia coli - enzymology Escherichia coli - physiology Escherichia coli Proteins Histidine Kinase Membrane Proteins - metabolism Methyl-Accepting Chemotaxis Proteins Phosphoenolpyruvate Sugar Phosphotransferase System - metabolism Phosphorylation Phosphotransferase system Salmonella typhimurium - enzymology Salmonella typhimurium - physiology |
| title | Investigation of transphosphorylation between chemotaxis proteins and the phosphoenolpyruvate: sugar phosphotransferase system |
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