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dc.contributor.author Augustus, AM
dc.contributor.author Sage, H
dc.contributor.author Spicer, LD
dc.coverage.spatial United States
dc.date.accessioned 2011-06-21T17:22:11Z
dc.date.issued 2010-04-20
dc.identifier http://www.ncbi.nlm.nih.gov/pubmed/20196619
dc.identifier.citation Biochemistry, 2010, 49 (15), pp. 3289 - 3295
dc.identifier.uri http://hdl.handle.net/10161/4018
dc.description.abstract We have used analytical ultracentrifugation to characterize the binding of the methionine repressor protein, MetJ, to synthetic oligonucleotides containing zero to five specific recognition sites, called metboxes. For all lengths of DNA studied, MetJ binds more tightly to repeats of the consensus sequence than to naturally occurring metboxes, which exhibit a variable number of deviations from the consensus. Strong cooperative binding occurs only in the presence of two or more tandem metboxes, which facilitate protein-protein contacts between adjacent MetJ dimers, but weak affinity is detected even with DNA containing zero or one metbox. The affinity of MetJ for all of the DNA sequences studied is enhanced by the addition of SAM, the known cofactor for MetJ in the cell. This effect extends to oligos containing zero or one metbox, both of which bind two MetJ dimers. In the presence of a large excess concentration of metbox DNA, the effect of cooperativity is to favor populations of DNA oligos bound by two or more MetJ dimers rather than a stochastic redistribution of the repressor onto all available metboxes. These results illustrate the dynamic range of binding affinity and repressor assembly that MetJ can exhibit with DNA and the effect of the corepressor SAM on binding to both specific and nonspecific DNA.
dc.format.extent 3289 - 3295
dc.language ENG
dc.language.iso en_US en_US
dc.relation.ispartof Biochemistry
dc.relation.isversionof 10.1021/bi902011f
dc.subject Bacterial Proteins
dc.subject Base Sequence
dc.subject Consensus Sequence
dc.subject DNA
dc.subject Dimerization
dc.subject Fractionation, Field Flow
dc.subject Kinetics
dc.subject Methionine
dc.subject Molecular Weight
dc.subject Oligodeoxyribonucleotides
dc.subject Protein Binding
dc.subject Repressor Proteins
dc.subject S-Adenosylmethionine
dc.subject Ultracentrifugation
dc.title Binding of MetJ repressor to specific and nonspecific DNA and effect of S-adenosylmethionine on these interactions.
dc.title.alternative en_US
dc.type Journal Article
dc.description.version Version of Record en_US
duke.date.pubdate 2010-4-20 en_US
duke.description.endpage 3295 en_US
duke.description.issue 15 en_US
duke.description.startpage 3289 en_US
duke.description.volume 49 en_US
dc.relation.journal Biochemistry en_US
pubs.author-url http://www.ncbi.nlm.nih.gov/pubmed/20196619
pubs.issue 15
pubs.organisational-group /Duke
pubs.organisational-group /Duke/School of Medicine
pubs.organisational-group /Duke/School of Medicine/Basic Science Departments
pubs.organisational-group /Duke/School of Medicine/Basic Science Departments/Biochemistry
pubs.organisational-group /Duke/School of Medicine/Clinical Science Departments
pubs.organisational-group /Duke/School of Medicine/Clinical Science Departments/Radiology
pubs.organisational-group /Duke/School of Medicine/Institutes and Centers
pubs.organisational-group /Duke/School of Medicine/Institutes and Centers/Duke Cancer Institute
pubs.organisational-group /Duke/School of Medicine/Institutes and Centers/Duke Human Vaccine Institute
pubs.publication-status Published
pubs.volume 49
dc.identifier.eissn 1520-4995

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