RecOR complex including RecR N-N dimer and RecO monomer displays a high affinity for ssDNA
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چکیده
منابع مشابه
RecOR complex including RecR N-N dimer and RecO monomer displays a high affinity for ssDNA
RecR is an important recombination mediator protein in the RecFOR pathway. RecR together with RecO and RecF facilitates RecA nucleoprotein filament formation and homologous pairing. Structural and biochemical studies of Thermoanaerobacter tengcongensis RecR (TTERecR) and its series mutants revealed that TTERecR uses the N-N dimer as a basic functional unit to interact with TTERecO monomer. Two ...
متن کاملRecFOR and RecOR as distinct RecA loading pathways.
The molecular role of the RecF protein in loading RecA protein onto single-stranded DNA (ssDNA)-binding protein-coated ssDNA has been obscured by the facility with which the RecO and RecR proteins alone perform this function. We now show that RecFOR and RecOR define distinct RecA loading functions that operate optimally in different contexts. RecFOR, but not RecOR, is most effective when RecF(R...
متن کاملSSB protein limits RecOR binding onto single-stranded DNA.
The RecO and RecR proteins form a complex that promotes the nucleation of RecA protein filaments onto SSB protein-coated single-stranded DNA (ssDNA). However, even when RecO and RecR proteins are provided at optimal concentrations, the loading of RecA protein is surprisingly slow, typically proceeding with a lag of 10 min or more. The rate-limiting step in RecOR-promoted RecA nucleation is the ...
متن کاملThe process of displacing the single-stranded DNA-binding protein from single-stranded DNA by RecO and RecR proteins
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...
متن کاملRecA protein filaments: end-dependent dissociation from ssDNA and stabilization by RecO and RecR proteins.
RecA protein filaments formed on circular (ssDNA) in the presence of ssDNA binding protein (SSB) are generally stable as long as ATP is regenerated. On linear ssDNA, stable RecA filaments are believed to be formed by nucleation at random sites on the DNA followed by filament extension in the 5' to 3' direction. This view must now be enlarged as we demonstrate that RecA filaments formed on linea...
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ژورنال
عنوان ژورنال: Nucleic Acids Research
سال: 2012
ISSN: 1362-4962,0305-1048
DOI: 10.1093/nar/gks889