An extended DNA structure through deoxyribose-base stacking induced by RecA protein
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چکیده
منابع مشابه
An extended DNA structure through deoxyribose-base stacking induced by RecA protein.
The family of proteins that are homologous to RecA protein of Escherichia coli is essential to homologous genetic recombination in various organisms including viruses, bacteria, lower eukaryotes, and mammals. In the presence of ATP (or ATPgammaS), these proteins form helical filaments containing single-stranded DNA at the center. The single-stranded DNA bound to RecA protein is extended 1.5 tim...
متن کاملKinetics of base stacking-aided DNA hybridization.
The association and dissociation rate constants (k(a) and k(d)) of DNA hybridizations involving dual, single or no stacking with different base-pairing sizes were measured, which reveals the advantage of stacking hybridization in both the kinetic and steady state.
متن کاملTriple-helical DNA pairing intermediates formed by recA protein.
RecA protein aligns homologous single- and double-stranded DNA molecules in three-stranded joints that can extend over thousands of base pairs. When cross-linked by 4'-amino-4,5',8-trimethyl-psoralen the joint structure observed in nonuniform and divided into multiple substructures each a few hundred base pairs long. Two paired substructures are observed; at least one, and possibly both, are ri...
متن کاملExtent of duplex DNA underwinding induced by RecA protein binding in the presence of ATP.
A method is described for the accurate determination of the superhelical density (omega) of highly underwound circular DNA molecules. Using this method, duplex DNA bound by RecA protein in the presence of ATP at pH 7.5 is found to be underwound by 39.6% (omega = -0.396), corresponding to a helical periodicity of 17.4 base-pairs per turn. The underwinding is increased to 41% (17.9 base-pairs per...
متن کاملAsymmetry in the recA protein-DNA filament.
The apparent DNA site size obtained from an assay monitoring the ATPase activity of Escherichia coli recA protein (n = 3.5) differs from that determined from a direct DNA binding assay (n = 7) done under identical conditions. Investigation of this discrepancy indicates that at a DNA:protein ratio of 3.5:1, one-half of the recA protein population is less sensitive to ATPase activity inhibition b...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1997
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.94.13.6623