Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

DNA structural elements required for FEN-1 binding

J J Harrington1, M R Lieber

  • 1Department of Pathology, Stanford University School of Medicine, California 94305.

The Journal of Biological Chemistry
|March 3, 1995
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Generation of cell lines for drug discovery through random activation of gene expression: application to the human histamine H3 receptor.

Assay and drug development technologies·2005
Same author

DNA length-dependent cooperative interactions in the binding of Ku to DNA.

Biochemistry·2001
Same author

Analysis of the V(D)J recombination efficiency at lymphoid chromosomal translocation breakpoints.

The Journal of biological chemistry·2001
Same author

Creation of genome-wide protein expression libraries using random activation of gene expression.

Nature biotechnology·2001
Same author

The mammalian FEN-1 locus: structure and conserved sequence features.

Microbial & comparative genomics·2001
Same author

Colorectal cancer screening by detection of altered human DNA in stool: feasibility of a multitarget assay panel.

Gastroenterology·2000
Same journal

Isotope-Edited ESEEM: A New Method for Probing Copper Binding Sites in Neurodegenerative Proteins.

The Journal of biological chemistry·2026
Same journal

Introduction to the Thematic Review Series on Intracellular Protein Degradation. The ubiquitous biology of intracellular protein degradation: a tribute to Alfred L. ("Fred") Goldberg.

The Journal of biological chemistry·2026
Same journal

Correction: Aromatic residue-rich amino-terminal segments of temporin L self-assemble into collagen-mimetic peptides with cell-adhesion properties.

The Journal of biological chemistry·2026
Same journal

YhbO is a DJ-1 family glyoxalase and α-oxoaldehyde hydratase that confers resistance to reactive carbonyl stress (112).

The Journal of biological chemistry·2026
Same journal

ARMH3 acts as a central scaffold at the Golgi/TGN through interactions with Arl5, GBF1, and PI4KB.

The Journal of biological chemistry·2026
Same journal

PAX8 controls proximal tubule epithelial identity and stress response through epigenetic modification of distal regulatory elements.

The Journal of biological chemistry·2026
See all related articles

Flap endonuclease-1 (FEN-1) binds and cleaves DNA flap structures. The adjacent strand (Fadj) is crucial for FEN-1 binding and activity, acting as a double-stranded template for substrate recognition.

Area of Science:

  • Molecular Biology
  • Enzymology
  • DNA Repair

Background:

  • Eukaryotic cells possess FEN-1 (flap endonuclease-1), a 42-kDa enzyme with 5'-flap DNA endonuclease and 5'-exonuclease activities.
  • FEN-1 shares homology with structure-specific nucleases like human XP-G and yeast RAD2/YKL510, all recognizing branched DNA structures (DNA flaps).

Purpose of the Study:

  • To identify key structural determinants for FEN-1's recognition and cleavage of DNA flap structures.
  • To elucidate the role of the adjacent strand (Fadj) in FEN-1-DNA substrate interactions.

Main Methods:

  • Development of a mobility shift assay to study DNA flap structures.
  • Investigation of FEN-1 binding and cleavage efficiency with varying Fadj strand presence and position.
  • Analysis of double flap structures to understand Fadj strand function.

Related Experiment Videos

Main Results:

  • The Fadj strand is essential for efficient FEN-1 binding and cleavage of DNA flap structures.
  • Recessed or absent Fadj strands significantly reduce FEN-1 binding efficiency.
  • The Fadj strand serves as a double-stranded template for FEN-1 binding near the flap's elbow.

Conclusions:

  • FEN-1's substrate recognition is critically dependent on the presence and positioning of the Fadj strand.
  • The Fadj strand facilitates FEN-1 binding by providing a necessary double-stranded DNA template.
  • These findings enhance understanding of how structure-specific nucleases like FEN-1 interact with diverse DNA substrates.