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• W2058654089 endingPage "5818" @default.
• W2058654089 startingPage "5809" @default.
• W2058654089 abstract "Pif1p is the prototypical member of the PIF1 family of DNA helicases, a subfamily of SFI helicases conserved from yeast to humans. Baker's yeast Pif1p is involved in the maintenance of mitochondrial, ribosomal and telomeric DNA and may also have a general role in chromosomal replication by affecting Okazaki fragment maturation. Here we investigate the substrate preferences for Pif1p. The enzyme was preferentially active on RNA–DNA hybrids, as seen by faster unwinding rates on RNA–DNA hybrids compared to DNA–DNA hybrids. When using forked substrates, which have been shown previously to stimulate the enzyme, Pif1p demonstrated a preference for RNA–DNA hybrids. This preferential unwinding could not be correlated to preferential binding of Pif1p to the substrates that were the most readily unwound. Although the addition of the single-strand DNA-binding protein replication protein A (RPA) stimulated the helicase reaction on all substrates, it did not diminish the preference of Pif1p for RNA–DNA substrates. Thus, forked RNA–DNA substrates are the favored substrates for Pif1p in vitro . We discuss these findings in terms of the known biological roles of the enzyme." @default.
• W2058654089 created "2016-06-24" @default.
• W2058654089 creator A5006524357 @default.
• W2058654089 creator A5025770177 @default.
• W2058654089 date "2007-08-23" @default.
• W2058654089 modified "2023-09-27" @default.
• W2058654089 title "The yeast Pif1p DNA helicase preferentially unwinds RNA DNA substrates" @default.
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• W2058654089 doi "https://doi.org/10.1093/nar/gkm613" @default.
• W2058654089 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2034482" @default.
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• W2058654089 hasPublicationYear "2007" @default.
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