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Structure of the DNA repair and replication endonuclease and exonuclease fen-1: Coupling DNA and pcna binding to fen-1 activity

Academic Article
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Overview

related to degree

  • Hosfield, David J, Ph.D. in Macromolecular and Cellular Structure and Chemistry, Scripps Research 1996 - 2001

authors

  • Hosfield, David J
  • Mol, C. D.
  • Shen, B. H.
  • Tainer, John

publication date

  • October 1998

journal

  • Cell  Journal

abstract

  • Flap endonuclease (FEN-1) removes 5' overhanging flaps in DNA repair and processes the 5' ends of Okazaki fragments in lagging strand DNA synthesis. The crystal structure of Pyrococcus furiosus FEN-1, active-site metal ions, and mutational information indicate interactions for the single- and double-stranded portions of the flap DNA substrate and identify an unusual DNA-binding motif. The enzyme's active-site structure suggests that DNA binding induces FEN-1 to clamp onto the cleavage junction to form the productive complex. The conserved FEN-1 C terminus binds proliferating cell nuclear antigen (PCNA) and positions FEN-1 to act primarily as an exonuclease in DNA replication, in contrast to its endonuclease activity in DNA repair. FEN-1 mutations altering PCNA binding should reduce activity during replication, likely causing DNA repeat expansions as seen in some cancers and genetic diseases.

subject areas

  • Amino Acid Sequence
  • Binding Sites
  • Catalysis
  • DNA
  • DNA Repair
  • DNA Replication
  • Endodeoxyribonucleases
  • Endonucleases
  • Exodeoxyribonuclease V
  • Exodeoxyribonucleases
  • Exonucleases
  • Flap Endonucleases
  • Ions
  • Magnesium
  • Molecular Sequence Data
  • Proliferating Cell Nuclear Antigen
  • Protein Conformation
  • Pyrococcus furiosus
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Identity

International Standard Serial Number (ISSN)

  • 0092-8674

Digital Object Identifier (DOI)

  • 10.1016/s0092-8674(00)81789-4

PubMed ID

  • 9778254
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Additional Document Info

start page

  • 135

end page

  • 146

volume

  • 95

issue

  • 1

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