4/12/2023 0 Comments 32 strand dna activationThese findings provide new insights on mechanisms of helicase regulation by accessory proteins. A point mutation at a regulatory DNA binding site on XPD similarly activates this switch. Here, optical trap measurements of the unwinding activity of a single XPD helicase in the presence of RPA2 reveal a mechanism in which XPD interconverts between two states with different processivities and transient RPA2 interactions stabilize the more processive state, activating a latent ‘processivity switch’ in XPD. Ferroplasma acidarmanus xeroderma pigmentosum group D (XPD) helicase serves as a model for understanding the molecular mechanisms of superfamily 2B helicases, and its activity is enhanced by the cognate single-stranded DNA binding protein replication protein A 2 (RPA2). ![]() Such encounters regulate helicase function, although the underlying mechanisms remain largely unknown. In the cell, helicases function in the context of other NA-associated proteins such as single-stranded DNA binding proteins. Helicases utilize nucleotide triphosphate (NTP) hydrolysis to translocate along single-stranded nucleic acids (NA) and unwind the duplex.
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