Disease relevance of helicase

• Replacement of gly815 in helicase motif V alters the single-stranded DNA-dependent ATPase activity of the herpes simplex virus type 1 helicase-primase [1].
• Although the UL5(G815A) protein does not support viral DNA replication in vivo, the purified UL5(G815A).52 subcomplex retains primase and helicase activities and supports strand displacement DNA synthesis on a preformed replication fork in the presence of the other HSV-1 replication proteins [1].
• We have shown previously that when a short DNA sequence within AcMNPV ORF95, which encodes the viral helicase P143, is replaced with the colinear region of B. mori nucleopolyhedrovirus (BmNPV), AcMNPV gains the ability to replicate in Bm5 cells [2].
• These results provide further evidence that baculovirus helicase genes encode proteins with biochemical properties similar to those of classical DNA helicases [3].
• Hepatitis C virus (HCV) NS3 protein contains at least three enzymatic activities: NS2-3 protease, NS3 serine protease, and NTPase/RNA helicase [4].

High impact information on helicase

• By means of site-directed mutagenesis, we demonstrated that NS3a/NS3b cleavage occurs within the RNA helicase sequence motif that is highly conserved in the Flaviviridae family and that neither NS2-3 protease nor NS3 serine protease was responsible for this cleavage [4].

References