The KH domain facilitates the substrate specificity and unwinding processivity of DDX43 helicase
Manisha Yadav, Ravi Shankar Singh, Daniel J. Hogan, Venkatasubramanian Vidhyasagar, Shizhuo Yang, Ivy Yeuk Wah Chung, Anthony Kusalik, Oleg Y. Dmitriev, Mirosław Cygler, Yuliang Wu
Abstract
N-heteronuclear single quantum coherence NMR, the optimal binding sequence was identified as TTGT. Finally, we found that the full-length DDX43 helicase prefers DNA or RNA substrates with TTGT or UUGU single-stranded tails and that the KH domain is critically important for sequence specificity and unwinding processivity. Collectively, our results demonstrated that the KH domain facilitates the substrate specificity and processivity of the DDX43 helicase.
Topics & Concepts
ProcessivityHelicaseSubstrate (aquarium)Domain (mathematical analysis)BiophysicsCell biologyChemistryBiologyBiochemistryDNAGeneRNAMathematicsDNA replicationMathematical analysisEcologyDNA Repair MechanismsPlant Genetic and Mutation StudiesRNA and protein synthesis mechanisms