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| pubmed-article:10644772 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:10644772 | pubmed:dateCreated | 2000-2-29 | lld:pubmed |
| pubmed-article:10644772 | pubmed:abstractText | The gamma complex of the Escherichia coli DNA polymerase III holoenzyme assembles the beta sliding clamp onto DNA in an ATP hydrolysis-driven reaction. Interactions between gamma complex and primer/template DNA are investigated using fluorescence depolarization to measure binding of gamma complex to different DNA substrates under steady-state and presteady-state conditions. Surprisingly, gamma complex has a much higher affinity for single-stranded DNA (K(d) in the nM range) than for a primed template (K(d) in the microM range) under steady-state conditions. However, when examined on a millisecond time scale, we find that gamma complex initially binds very rapidly and with high affinity to primer/template DNA but is converted subsequently to a much lower affinity DNA binding state. Presteady-state data reveals an effective dissociation constant of 1.5 nM for the initial binding of gamma complex to DNA and a dissociation constant of 5.7 microM for the low affinity DNA binding state. Experiments using nonhydrolyzable ATPgammaS show that ATP binding converts gamma complex from a low affinity "inactive" to high affinity "active" DNA binding state while ATP hydrolysis has the reverse effect, thus allowing cycling between active and inactive DNA binding forms at steady-state. We propose that a DNA-triggered switch between active and inactive states of gamma complex provides a two-tiered mechanism enabling gamma complex to recognize primed template sites and load beta, while preventing gamma complex from competing with DNA polymerase III core for binding a newly loaded beta.DNA complex. | lld:pubmed |
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| pubmed-article:10644772 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10644772 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10644772 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10644772 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10644772 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:10644772 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:10644772 | pubmed:author | pubmed-author:GoodmanM FMF | lld:pubmed |
| pubmed-article:10644772 | pubmed:author | pubmed-author:O'DonnellMM | lld:pubmed |
| pubmed-article:10644772 | pubmed:author | pubmed-author:BeechemJ MJM | lld:pubmed |
| pubmed-article:10644772 | pubmed:author | pubmed-author:BloomL BLB | lld:pubmed |
| pubmed-article:10644772 | pubmed:author | pubmed-author:HingoraniM... | lld:pubmed |
| pubmed-article:10644772 | pubmed:author | pubmed-author:BertramJ GJG | lld:pubmed |
| pubmed-article:10644772 | pubmed:author | pubmed-author:AsonBB | lld:pubmed |
| pubmed-article:10644772 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10644772 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:10644772 | pubmed:volume | 275 | lld:pubmed |
| pubmed-article:10644772 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10644772 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10644772 | pubmed:pagination | 3006-15 | lld:pubmed |
| pubmed-article:10644772 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:10644772 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10644772 | pubmed:articleTitle | A model for Escherichia coli DNA polymerase III holoenzyme assembly at primer/template ends. DNA triggers a change in binding specificity of the gamma complex clamp loader. | lld:pubmed |
| pubmed-article:10644772 | pubmed:affiliation | Department of Chemistry, Arizona State University, Tempe, Arizona 85287-1604, USA. | lld:pubmed |
| pubmed-article:10644772 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10644772 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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