{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T11:26:42Z","timestamp":1790076402871,"version":"4.0.1"},"reference-count":51,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2019,11,11]],"date-time":"2019-11-11T00:00:00Z","timestamp":1573430400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["GM29963"],"award-info":[{"award-number":["GM29963"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2020,2]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Methylation of specific chemoreceptor glutamyl residues by methyltransferase CheR mediates sensory adaptation and gradient sensing in bacterial chemotaxis. Enzyme action is a function of chemoreceptor signaling conformation: kinase\u2010off receptors are more readily methylated than kinase\u2010on, a feature central to adaptational and gradient\u2010sensing mechanisms. Differential enzyme action could reflect differential binding, catalysis or both. We investigated by measuring CheR binding to kinase\u2010off and kinase\u2010on forms of\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    aspartate receptor Tar deleted of its CheR\u2010tethering, carboxyl terminus pentapeptide. This allowed characterization of the low\u2010affinity binding of enzyme to the substrate receptor body, otherwise masked by high\u2010affinity interaction with pentapeptide. We quantified the low\u2010affinity protein\u2013protein interactions by determining kinetic rate constants of association and dissociation using bio\u2010layer interferometry and from those values calculating equilibrium constants. Whether Tar signaling conformations were shifted by ligand occupancy or adaptational modification, there was little or no difference between the two signaling conformations in kinetic or equilibrium parameters of enzyme\u2010receptor binding. Thus, differential methyltransferase action does not reflect differential binding. Instead, the predominant determinants of binding must be common to different signaling conformations. Characterization of the dependence of association rate constants on Deybe length, a measure of the influence of electrostatics, implicated electrostatic interactions as a common binding determinant. Taken together, our observations indicate that differential action of methyltransferase on kinase\u2010off and kinase\u2010on chemoreceptors is not the result of differential binding and suggest it reflects differential catalytic propensity. Differential catalysis rather than binding could well be central to other enzymes distinguishing alternative conformations of protein substrates.\n                  <\/jats:p>","DOI":"10.1002\/pro.3760","type":"journal-article","created":{"date-parts":[[2019,10,25]],"date-time":"2019-10-25T22:58:07Z","timestamp":1572044287000},"page":"443-454","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":15,"title":["Methyltransferase CheR binds to its chemoreceptor substrates independent of their signaling conformation yet modifies them differentially"],"prefix":"10.1002","volume":"29","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-3371-1023","authenticated-orcid":false,"given":"Mingshan","family":"Li","sequence":"first","affiliation":[{"name":"Department of Biochemistry University of Missouri\u2010Columbia  Columbia Missouri"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2449-2663","authenticated-orcid":false,"given":"Gerald L.","family":"Hazelbauer","sequence":"additional","affiliation":[{"name":"Department of Biochemistry University of Missouri\u2010Columbia  Columbia Missouri"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2019,11,11]]},"reference":[{"key":"e_1_2_8_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.tibs.2007.09.014"},{"key":"e_1_2_8_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.mib.2009.12.014"},{"key":"e_1_2_8_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.tim.2015.03.003"},{"key":"e_1_2_8_5_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi971510h"},{"key":"e_1_2_8_6_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi9713207"},{"key":"e_1_2_8_7_1","doi-asserted-by":"crossref","first-page":"15638","DOI":"10.1016\/S0021-9258(18)55445-4","article-title":"Mutations in the aspartate receptor of Escherichia coli which affect aspartate binding","volume":"265","author":"Mowbray SL","year":"1990","journal-title":"J Biol Chem"},{"key":"e_1_2_8_8_1","doi-asserted-by":"publisher","DOI":"10.1128\/JB.01391-09"},{"key":"e_1_2_8_9_1","doi-asserted-by":"publisher","DOI":"10.1128\/jb.171.7.3609-3618.1989"},{"key":"e_1_2_8_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0969-2126(97)00210-4"},{"key":"e_1_2_8_11_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jsb.2014.03.015"},{"key":"e_1_2_8_12_1","doi-asserted-by":"publisher","DOI":"10.1110\/ps.4640102"},{"key":"e_1_2_8_13_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.1660187"},{"key":"e_1_2_8_14_1","doi-asserted-by":"crossref","first-page":"10378","DOI":"10.1016\/S0021-9258(18)34030-4","article-title":"The methyl\u2010accepting chemotaxis proteins of Escherichia coli. 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