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Escherichia coli RecBC helicase has two translocase activities controlled by a single ATPase motor.


ABSTRACT: E. coli RecBCD is a DNA helicase with two ATPase motors (RecB, a 3'?5' translocase, and RecD, a 5'?3' translocase) that function in repair of double-stranded DNA breaks. The RecBC heterodimer, with only the RecB motor, remains a processive helicase. Here we examined RecBC translocation along single-stranded DNA (ssDNA). Notably, we found RecBC to have two translocase activities: the primary translocase moves 3'?5', whereas the secondary translocase moves RecBC along the opposite strand of a forked DNA at a similar rate. The secondary translocase is insensitive to the ssDNA backbone polarity, and we propose that it may fuel RecBCD translocation along double-stranded DNA ahead of the unwinding fork and ensure that the unwound single strands move through RecBCD at the same rate after interaction with a crossover hot-spot indicator (Chi) sequence.

SUBMITTER: Wu CG 

PROVIDER: S-EPMC2950890 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature

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Escherichia coli RecBC helicase has two translocase activities controlled by a single ATPase motor.

Wu Colin G CG   Bradford Christina C   Lohman Timothy M TM  

Nature structural & molecular biology 20100919 10


E. coli RecBCD is a DNA helicase with two ATPase motors (RecB, a 3'→5' translocase, and RecD, a 5'→3' translocase) that function in repair of double-stranded DNA breaks. The RecBC heterodimer, with only the RecB motor, remains a processive helicase. Here we examined RecBC translocation along single-stranded DNA (ssDNA). Notably, we found RecBC to have two translocase activities: the primary translocase moves 3'→5', whereas the secondary translocase moves RecBC along the opposite strand of a fork  ...[more]

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