Characterization of the enzymatic properties of the yeast Dna2 helicase/endonuclease suggests a new model for Okazaki fragment processing

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The Saccharomyces cerevisiae Dna2, which contains single-stranded DNA-specific endonuclease activity, interacts genetically and physically with Fen-l, a structure-specific endonuclease implicated in Okazaki fragment maturation during lagging strand synthesis. In this report, we investigated the properties of the Dna2 helicase/endonuclease activities in search of their in vivo physiological functions in eukaryotes. We found that the Dnaa helicase activity translocates in the 5' to 3' direction and uses DNA with free ends as the preferred substrate. Furthermore, the endonucleolytic cleavage activity of Dna2 was markedly stimulated, by the presence of an RNA segment at the 5'-end of single-stranded DNA and occurred within the DNA, ensuring the complete removal of the initiator RNA segment on the Okazaki fragment. In addition, we demonstrated that the removal of pre-existing initiator 5'-terminal RNA segments depended on a displacement reaction carried out during the DNA polymerase delta -catalyzed elongation of the upstream Okazaki fragments. These properties indicate that Dna2 is well suited to remove the primer RNA on the Okazaki fragment. Based op this information, we propose a new model in which Dna2 plays a direct role in Okazaki fragment maturation in conjunction with Fen-l.
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Issue Date
2000-12
Language
ENG
Article Type
Article
Keywords

BASE EXCISION-REPAIR; SINGLE-STRANDED-DNA; PROKARYOTIC RNASE HII; REPLICATION FACTOR-C; SACCHAROMYCES-CEREVISIAE; SV40 ORIGIN; SCHIZOSACCHAROMYCES-POMBE; ENDONUCLEASE ACTIVITY; HELICASE; RAD27

Citation

JOURNAL OF BIOLOGICAL CHEMISTRY, v.275, no.48, pp.38022 - 38031

ISSN
0021-9258
DOI
10.1074/jbc.M006513200
URI
http://hdl.handle.net/10203/74830
Appears in Collection
BS-Journal Papers(저널논문)
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