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

Title
The N-terminal 45-kDa Domain of Dna2 Endonuclease/Helicase Targets the Enzyme to Secondary Structure DNA
Authors
배성호
Issue Date
2013
Publisher
JOURNAL OF BIOLOGICAL CHEMISTRY
Series/Report no.
JOURNAL OF BIOLOGICAL CHEMISTRY ; Vol288 no.13 Startpage 9468 Endpage 9481
Abstract
Background: The biochemical function of variable N-terminal regions of eukaryotic Dna2 remains unclear. Results: The N-terminal 45-kDa domain of yeast Dna2 targets the enzyme specifically to a secondary structure flap. Conclusion: The hairpin binding activity of Dna2 contributes to efficient removal of hairpin flaps together with endonuclease and helicase activities during Okazaki fragment processing. Significance: The hairpin binding activity of Dna2 is critical for genome stability.
URI
http://dspace.inha.ac.kr/handle/10505/33239
ISSN
0021-9258
Appears in Collections:
College of Natural Science(자연과학대학) > Biological Sciences (생명과학) > Local Access Journal Papers, Reports(생명과학 논문, 보고서)

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