Show simple item record

dc.contributor.authorMyers, Lawrence C.
dc.contributor.authorJackow, François
dc.contributor.authorVerdine, Gregory L.
dc.date.accessioned2019-10-09T13:56:50Z
dc.date.issued1995
dc.identifier.citationMyers, Lawrence C., François Jackow, and Gregory L. Verdine. 1995. “Metal Dependence of Transcriptional Switching in Escherichia ColiAda.” Journal of Biological Chemistry270 (12): 6664–70. https://doi.org/10.1074/jbc.270.12.6664.
dc.identifier.issn0021-9258
dc.identifier.issn1083-351X
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:41511277*
dc.description.abstractThe Escherichia coli Ada protein repairs methylphos photriesters in DNA by direct, irreversible methyl transfer to one of its own cysteine residues. The methyl transfer process is autocatalyzed by coordination of the acceptor residue, Cys(69), to, a tightly bound zinc ion. Kinetic data reveal a 4-fold reduction in the methylphosphotriester repair activity for the Cd(II) form of Ada versus the native Zn(II)-bound form, thus confirming a direct role for the metal in autocatalysis. Quantitative electrophoretic mobility shift assays reveal that the specific DNA affinity of the protein is increased 10(3)-fold by transfer of a methyl group to Cys(69); the Cd(II) and the Zn(II) forms of the protein behave similarly in this respect, This methylation-sensitive stimulation of binding underlies the ability of Ada to activate inducibly the transcription of a methylation-dependent regulon, We conclude that the chemical properties of the bound metal influence the transition state for autocatalytic methyl transfer, but not the structure that ultimately results from this process.
dc.language.isoen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology
dash.licenseLAA
dc.titleMetal Dependence of Transcriptional Switching in Escherichia coli Ada
dc.typeJournal Article
dc.description.versionVersion of Record
dc.relation.journalThe Journal of Biological Chemistry
dash.depositing.authorVerdine, Gregory L.::b80a6eb8a9fb2d98773ce5b5cc1dd993::600
dc.date.available2019-10-09T13:56:50Z
dash.workflow.comments1Science Serial ID 105130
dc.identifier.doi10.1074/jbc.270.12.6664
dash.source.volume270;12
dash.source.page6664-6670


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record