Binding of substrate locks the electrochemistry of CRY-DASH into DNA repair

Yvonne M. Gindt, Adriana Messyasz, Pamela I. Jumbo

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

VcCry1, a member of the CRY-DASH family, may serve two diverse roles in vivo, including blue-light signaling and repair of UV-damaged DNA. We have discovered that the electrochemistry of the flavin adenine dinucleotide cofactor of VcCry1 is locked to cycle only between the hydroquinone and neutral semiquinone states when UV-damaged DNA is present. Other potential substrates, including undamaged DNA and ATP, have no discernible effect on the electrochemistry, and the kinetics of the reduction is unaffected by damaged DNA. Binding of the damaged DNA substrate determines the role of the protein and prevents the presumed photochemistry required for blue-light signaling.

Original languageEnglish
Pages (from-to)2802-2805
Number of pages4
JournalBiochemistry
Volume54
Issue number18
DOIs
StatePublished - 12 May 2015

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