Ontology highlight
ABSTRACT:
SUBMITTER: Gloor JW
PROVIDER: S-EPMC2966106 | biostudies-literature | 2010 Nov
REPOSITORIES: biostudies-literature
Gloor Jason W JW Balakrishnan Lata L Bambara Robert A RA
The Journal of biological chemistry 20100825 45
FEN1 cleaves 5' flaps at their base to create a nicked product for ligation. FEN1 has been reported to enter the flap from the 5'-end and track to the base. Current binding analyses support a very different mechanism of interaction with the flap substrate. Measurements of FEN1 binding to a flap substrate show that the nuclease binds with similar high affinity to the base of a long flap even when the 5'-end is blocked with biotin/streptavidin. However, FEN1 bound to a blocked flap is more sensiti ...[more]