MCELLBI 110 Lecture Notes - Lecture 4: Escherichia Coli, Atp Hydrolysis, Flap Structure-Specific Endonuclease 1

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In the cell, helicases have loaders required to engage them on substrates: step wise movement of the helicase is powered by repeated cycles of atp hydrolysis. Unwinding occurs by the helicase tracking on either the 5"-3" of the 3"-5" strand. Dna helicase tracking on ssdna: atp hydrolysis driven hand over hand mechanism of dna helicase tracking on ssdna. Prokaryotic ssdna binding protein: ssb homotetramer, by coating the exposed ssdna, also prevents strand reannealing, thus maintain the template. Each subunit can independently bind and release ssdna, and rebind to an adjacent ssdna segment, resulting in tetramer sliding while overall remaining bound to dna, which allows pol iii to displace ssd. In e. coli rna primers are removal by dna pol i: 5"-3" exonuclease removes rna (and this enzymic activity is the essential function of. Dna pol i in e. coli: 5"-3" polymerase activity can replace with dna.

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