Abstract:
:FOXP2 is a member of the P subfamily of FOX transcription factors, the DNA-binding domain of which is the winged helix forkhead domain (FHD). In this work we show that the FOXP2 FHD is able to bind to various DNA sequences, including a novel sequence identified in this work, with different affinities and rates as detected using surface plasmon resonance. Combining the experimental work with molecular docking, we show that high-affinity sequences remain bound to the protein for longer, form a greater number of interactions with the protein and induce a greater structural change in the protein than low-affinity sequences. We propose a binding model for the FOXP2 FHD that involves three types of binding sequence: low affinity sites which allow for rapid scanning of the genome by the protein in a partially unstructured state; moderate affinity sites which serve to locate the protein near target sites and high-affinity sites which secure the protein to the DNA and induce a conformational change necessary for functional binding and the possible initiation of downstream transcriptional events.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Webb H,Steeb O,Blane A,Rotherham L,Aron S,Machanick P,Dirr H,Fanucchi Sdoi
10.1093/jb/mvx003subject
Has Abstractpub_date
2017-07-01 00:00:00pages
45-54issue
1eissn
0021-924Xissn
1756-2651pii
mvx003journal_volume
162pub_type
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