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UID:928@biology.technion.ac.il

DTSTART;TZID=Asia/Jerusalem:20201125T130000

DTEND;TZID=Asia/Jerusalem:20201125T140000

DTSTAMP:20210802T125902Z

URL:https://biology.technion.ac.il/en/seminars/m-sc-graduate-seminar-roi-s
 iegelman-2/

SUMMARY:M.Sc. Graduate Seminar-Roi Siegelman [No Categories]
DESCRIPTION:Location:   \n Affiliation: \n Host:\n A single molecule study 
 of theroles of the RecC subunit in DNA unwinding by RecBCD DNAdouble-stra
 nd breaks (DSBs) are the most cytotoxic of DNA lesions and theirrepair req
 uires a comprehensive and rapid cellular response. In EscherichiaColi\,Rec
 BCDinitiates the homologous recombination pathway for DSB repair by unwind
 ing theDNA at the damaged site rapidly and processively. Asingle-molecule 
 assay previously developed in our lab\, enabled monitoring theactivity of 
 the individual subunits\, as part of the full complex of RecBCD. Theresult
 s demonstrated that synergy between its subunits supports unwinding by Rec
 BCD.However\, how RecCcontributes to RecBCD'sunwinding activity has not ye
 t been fully understood. In my work\, I combinedsingle-molecule and in viv
 oassays to probe the activity of RecBCD mutated in their “pin” domain 
 within RecC\,which was suggested to split the duplex DNA before the indivi
 dual strands arepulled by RecB and RecD.  Our single molecule results rev
 eal that\,while the velocity is not significantly affected by these mutati
 ons\, the pindomain is crucial for the processivity of the whole complex a
 nd its subunits.Moreover\, the in vivoexperiments suggest that the process
 ivity determines the ability of RecBCD toefficiently initiate the repair r
 eaction.  

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