pubmed-article:12914783 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12914783 | lifeskim:mentions | umls-concept:C0034865 | lld:lifeskim |
pubmed-article:12914783 | lifeskim:mentions | umls-concept:C0243071 | lld:lifeskim |
pubmed-article:12914783 | lifeskim:mentions | umls-concept:C0243077 | lld:lifeskim |
pubmed-article:12914783 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:12914783 | pubmed:dateCreated | 2003-8-13 | lld:pubmed |
pubmed-article:12914783 | pubmed:abstractText | Cre recombinase exchanges DNA strands at the LoxP recognition site via transphosphorylation reactions that involve pentacoordinate transition states. We demonstrate that meta-vanadate ion (VO(3)(-)) and appropriate DNA substrates assemble a transition-state analog-like complex in the Cre active site. Meta-vanadate inhibits recombination of LoxP-derived oligonucleotide substrates that contain a gap at either or both scissile phosphates, but does not inhibit reactions with intact LoxP. The 3(')-hydroxyl group of the gapped substrate is required for inhibition, suggesting that vanadate is ligated by three oxo ligands. Assembly of the inhibited complex is slow (t(1/2)=19min at 4mM NaVO(3)) and requires Cre, substrates, and meta-vanadate. Holliday junction intermediates accumulated at lower meta-vanadate concentrations, suggesting that the second strand exchange is inhibited more readily than the first. The apparent K(D) for meta-vanadate is 1.5-2mM and binding shows positive cooperativity. This methodology may have general application for mechanistic studies of recombinase/topoisomerase-mediated strand exchange reactions. | lld:pubmed |
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pubmed-article:12914783 | pubmed:language | eng | lld:pubmed |
pubmed-article:12914783 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12914783 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12914783 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:12914783 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12914783 | pubmed:month | Aug | lld:pubmed |
pubmed-article:12914783 | pubmed:issn | 0006-291X | lld:pubmed |
pubmed-article:12914783 | pubmed:author | pubmed-author:MartinShelley... | lld:pubmed |
pubmed-article:12914783 | pubmed:author | pubmed-author:BaldwinEnoch... | lld:pubmed |
pubmed-article:12914783 | pubmed:author | pubmed-author:WachiShinichi... | lld:pubmed |
pubmed-article:12914783 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12914783 | pubmed:day | 29 | lld:pubmed |
pubmed-article:12914783 | pubmed:volume | 308 | lld:pubmed |
pubmed-article:12914783 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12914783 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12914783 | pubmed:pagination | 529-34 | lld:pubmed |
pubmed-article:12914783 | pubmed:dateRevised | 2010-12-3 | lld:pubmed |
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pubmed-article:12914783 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:12914783 | pubmed:articleTitle | Vanadate-based transition-state analog inhibitors of Cre-LoxP recombination. | lld:pubmed |
pubmed-article:12914783 | pubmed:affiliation | Section of Molecular and Cellular Biology, University of California, Davis 95616, USA. | lld:pubmed |
pubmed-article:12914783 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12914783 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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