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- W3138269779 abstract "The multifunctional phage replication protein gp43 is composed of an N-terminal prim-pol domain and a C-terminal domain similar to the SF4-type replicative helicases. We prepared four mutants all missing the prim-pol domain with the helicase core flanked by accessory N- and C-terminal regions truncated to varying extents. The shortest fragment still possessing strong ssDNA-dependent ATPase activity and helicase activity was gp43HEL519-983. The other proteins tested were gp43HEL557-983, gp43HEL519-855 and gp43HEL519-896. Removal of the 38 N-terminal residues in gp43HEL557-983, or the 128 and 87 C-terminal residues in gp43HEL519-855 and gp43HEL519-896, resulted in a significant decrease in the ATPase activities. The 38-amino acid N-terminal region has probably a function in modulating DNA binding and protein oligomerization. Deletion of the 87 C-terminal residues resulted in a twofold increase in the unwinding rate. This region is likely indispensable for binding to DNA substrates." @default.
- W3138269779 created "2021-03-29" @default.
- W3138269779 creator A5030550389 @default.
- W3138269779 creator A5059583385 @default.
- W3138269779 creator A5077703807 @default.
- W3138269779 creator A5078592269 @default.
- W3138269779 date "2021-06-01" @default.
- W3138269779 modified "2023-09-24" @default.
- W3138269779 title "The helicase core accessory regions of the phage BFK20 DnaB-like helicase gp43 significantly affect its activity, oligomeric state and DNA binding properties" @default.
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- W3138269779 doi "https://doi.org/10.1016/j.virol.2021.02.016" @default.
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