RecA binding to a single double-stranded DNA molecule: A possible role of DNA conformational fluctuations
نویسندگان
چکیده
منابع مشابه
RecA binding to a single double-stranded DNA molecule: a possible role of DNA conformational fluctuations.
Most genetic regulatory mechanisms involve protein-DNA interactions. In these processes, the classical Watson-Crick DNA structure sometimes is distorted severely, which in turn enables the precise recognition of the specific sites by the protein. Despite its key importance, very little is known about such deformation processes. To address this general question, we have studied a model system, n...
متن کاملRecA polymerization on double-stranded DNA by using single-molecule manipulation: the role of ATP hydrolysis.
The polymerization of RecA on individual double-stranded DNA molecules is studied. A linear DNA (lambda DNA, 48.5 Kb), anchored at one end to a cover glass and at the other end to an optically trapped 3-micrometers diameter polystyrene bead, serves as a template. The elongation caused by RecA assembly is measured in the presence of ATP and ATP[gammaS]. By using force extension and hydrodynamic ...
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The single-stranded DNA-binding protein (SSB protein) is required for efficient genetic recombination in vivo. One function for SSB protein in DNA strand exchange in vitro is to remove secondary structure from single-stranded DNA (ssDNA) and thereby aid in the formation of recA protein-saturated presynaptic complexes. In the preceding paper (Lavery, P. E., and Kowalczykowski, S. C. (1992) J. Bi...
متن کاملEffects of DNA sequence and structure on binding of RecA to single-stranded DNA.
Fluorescence anisotropy is used to follow the binding of RecA to short single-stranded DNA (ssDNA) sequences (39 bases) at low DNA and RecA concentration where the initial phase of polymerization occurs. We observe that RecA condensation is extremely sensitive to minute changes in DNA sequences. RecA binds strongly to sequences that are rich in pyrimidines and that lack significant secondary st...
متن کاملrecA protein-promoted DNA strand exchange. Stable complexes of recA protein and single-stranded DNA formed in the presence of ATP and single-stranded DNA binding protein.
The recA protein of Escherichia coli promotes the complete exchange of strands between full length linear duplex and single-stranded circular DNA molecules. An early step in this reaction consists of the binding of recA protein to single-stranded DNA. In the presence of ATP and the single-stranded DNA binding protein, recA protein and single-stranded DNA interact to form a complex whose stabili...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1998
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.95.21.12295