title: Post-translational control of protein function with light using a LOV-intein fusion protein.
abstract: Methods for the post-translational control of protein function with light hold much value as tools in cell biology. To this end, we report a fusion protein that consists of DnaE split-inteins, flanking the light sensitive LOV2 domain of Avena sativa. The resulting chimera combines the activities of these two unrelated proteins to enable controlled formation of a functional protein via upregulation of intein splicing with blue light in bacterial and human cells.
authors.affiliation: Chemistry, University of Southampton, Southampton, SO17 1BJ, UK. a.tavassoli@soton.ac.uk.
authors.forename: D C
authors.initials: DC
authors.lastname: Jones
authors.forename: I N
authors.initials: IN
authors.lastname: Mistry
authors.forename: A
authors.initials: A
authors.lastname: Tavassoli
mesh_terms: D000818:Animals; D002460:Cell Line; D004926:Escherichia coli; D006801:Humans; D047668:Inteins; D008027:Light; D008958:Models, Molecular; D011487:Protein Conformation / Q000528:radiation effects; D000072417:Protein Domains; D011499:Protein Processing, Post-Translational / Q000528:radiation effects*; D019154:Protein Splicing / Q000528:radiation effects