Linked Life Data

7494000

Source:http://linkedlifedata.com/resource/pubmed/id/7494000

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pubmed-article:7494000pubmed:abstractTextAn artificial operon that contains tandem holC-holD genes was used to overproduce a complex of the chi and psi subunits of the DNA polymerase III holoenzyme. Normally insoluble by itself, psi forms a tight soluble complex with chi. A purification procedure that yields pure, active chi psi complex in 100-mg quantities suitable for biophysical studies is reported. Sedimentation equilibrium studies demonstrate that chi psi is a 1:1 heterodimer. The presence of chi psi dramatically lowers the level of delta.delta' required to reconstitute holoenzyme to levels expected in vivo. That chi psi accomplishes this by binding to gamma or tau and increasing their affinity for delta.delta' was demonstrated by surface plasmon resonance using a Pharmacia BIA-core instrument. In the absence of delta.delta', chi psi binds to either the gamma or tau DnaX protein with Kd = 2 nM.lld:pubmed
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pubmed-article:7494000pubmed:authorpubmed-author:McHenryC SCSlld:pubmed
pubmed-article:7494000pubmed:authorpubmed-author:DallmannH GHGlld:pubmed
pubmed-article:7494000pubmed:authorpubmed-author:OlsonM WMWlld:pubmed
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pubmed-article:7494000pubmed:volume270lld:pubmed
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pubmed-article:7494000pubmed:pagination29570-7lld:pubmed
pubmed-article:7494000pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:7494000pubmed:year1995lld:pubmed
pubmed-article:7494000pubmed:articleTitleDnaX complex of Escherichia coli DNA polymerase III holoenzyme. The chi psi complex functions by increasing the affinity of tau and gamma for delta.delta' to a physiologically relevant range.lld:pubmed
pubmed-article:7494000pubmed:affiliationDepartment of Biochemistry, Biophysics and Genetics, University of Colorado Health Sciences Center, Denver 80262, USA.lld:pubmed
pubmed-article:7494000pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:7494000pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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