Ontology highlight
ABSTRACT:
SUBMITTER: Carter AR
PROVIDER: S-EPMC4937329 | biostudies-literature | 2016 Jul
REPOSITORIES: biostudies-literature
Carter Ashley R AR Seaberg Maasa H MH Fan Hsiu-Fang HF Sun Gang G Wilds Christopher J CJ Li Hung-Wen HW Perkins Thomas T TT
Nucleic acids research 20160524 12
RecBCD is a multifunctional enzyme that possesses both helicase and nuclease activities. To gain insight into the mechanism of its helicase function, RecBCD unwinding at low adenosine triphosphate (ATP) (2-4 μM) was measured using an optical-trapping assay featuring 1 base-pair (bp) precision. Instead of uniformly sized steps, we observed forward motion convolved with rapid, large-scale (∼4 bp) variations in DNA length. We interpret this motion as conformational dynamics of the RecBCD-DNA comple ...[more]