RecR-mediated Modulation of RecF Dimer Specificity for Single- and Double-stranded DNA
نویسندگان
چکیده
منابع مشابه
An interaction between the Escherichia coli RecF and RecR proteins dependent on ATP and double-stranded DNA.
The DNA binding and ATPase activities of RecF protein are modulated by RecR protein. Stoichiometric amounts of RecF protein bind to double-stranded (ds) DNA (about 1 RecF monomer/4-6 base pairs) in the presence of adenosine 5'-O-(3-thio)triphosphate (ATP gamma S), forming a homogeneous protein coating on the DNA. Little or no cooperativity is evident in the binding process. In the presence of A...
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The regions of single-stranded (ss) DNA that result from DNA damage are immediately coated by the ssDNA-binding protein (SSB). RecF pathway proteins facilitate the displacement of SSB from ssDNA, allowing the RecA protein to form protein filaments on the ssDNA region, which facilitates the process of recombinational DNA repair. In this study, we examined the mechanism of SSB displacement from s...
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In the presence of both the RecF and RecR proteins, RecA filament extension from a single strand gap into adjoining duplex DNA is attenuated. RecR protein alone has no effect, and RecF protein alone has a reduced activity. The RecFR complexes bind randomly, primarily to the duplex regions of the DNA, and the extension of the RecA filament is halted at the first complex encountered. A very slow ...
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Isolation of cell free fetal DNA (cffDNA) from maternal serum usually leads to very low concentrations of DNA impeding further resolving through conventional methods of electrophoresis. Although several protocols have been described for capillary electrophoresis (CE) of double stranded DNA, they usually need using special polymers or coated capillaries which degrade over time. Herein, we propos...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2009
ISSN: 0021-9258
DOI: 10.1074/jbc.m806378200