The N-terminal 45-kDa Domain of Dna2 Endonuclease/Helicase Targets the Enzyme to Secondary Structure DNA

Cited 12 time in webofscience Cited 0 time in scopus
  • Hit : 580
  • Download : 113
The removal of initiating primers from the 5'-ends of each Okazaki fragment, required for the generation of contiguous daughter strands, can be catalyzed by the combined action of DNA polymerase delta and Fen1. When the flaps generated by displacement of DNA synthesis activity of polymerase delta become long enough to bind replication protein A or form hairpin structures, the helicase/endonuclease enzyme, Dna2, becomes critical because of its ability to remove replication protein A-coated or secondary structure flaps. In this study, we show that the N-terminal 45-kDa domain of Dna2 binds hairpin structures, allowing the enzyme to target secondary structure flap DNA. We found that this activity was essential for the efficient removal of hairpin flaps by the endonuclease activity of Dna2 with the aid of its helicase activity. Thus, the efficient removal of hairpin structure flaps requires the coordinated action of all three functional domains of Dna2. We also found that deletion of the N-terminal 45-kDa domain of Dna2 led to a partial loss of the intra-S-phase checkpoint function and an increased rate of homologous recombination in yeast. We discuss the potential roles of the N-terminal domain of Dna2 in the maintenance of genomic stability.
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Issue Date
2013-03
Language
English
Article Type
Article
Keywords

OKAZAKI FRAGMENT MATURATION; STALLED REPLICATION FORKS; CELL NUCLEAR ANTIGEN; BREAK END RESECTION; ESSENTIAL IN-VIVO; SACCHAROMYCES-CEREVISIAE; POLYMERASE-DELTA; S-PHASE; FISSION YEAST; FLAP ENDONUCLEASE-1

Citation

JOURNAL OF BIOLOGICAL CHEMISTRY, v.288, no.13, pp.9468 - 9481

ISSN
0021-9258
DOI
10.1074/jbc.M112.418715
URI
http://hdl.handle.net/10203/173814
Appears in Collection
BS-Journal Papers(저널논문)
Files in This Item
000316862200063.pdf(2.1 MB)Download
This item is cited by other documents in WoS
⊙ Detail Information in WoSⓡ Click to see webofscience_button
⊙ Cited 12 items in WoS Click to see citing articles in records_button

qr_code

  • mendeley

    citeulike


rss_1.0 rss_2.0 atom_1.0