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| Content Provider | PubMed Central |
|---|---|
| Author | Martin, Shelley S. Wachi, Shinichiro Baldwin, Enoch P. |
| Copyright Year | 2003 |
| Abstract | 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 = 19 min at 4 mM NaVO3) 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 1.5–2 mM and binding shows positive cooperativity. This methodology may have general application for mechanistic studies of recombinase/topoisomerase-mediated strand exchange reactions. |
| Starting Page | 529 |
| File Format | |
| ISSN | 10902104 |
| e-ISSN | 10902104 |
| Journal | Biochemical and biophysical research communications |
| Issue Number | 3 |
| Volume Number | 308 |
| Language | English |
| Publisher Date | 2003-08-29 |
| Access Restriction | Open |
| Subject Keyword | Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Molecular Biology Biochemistry Biophysics |
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