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

A closed conformation for the Pol lambda catalytic cycle.

Miguel Garcia-Diaz1, Katarzyna Bebenek, Joseph M Krahn

  • 1Laboratory of Structural Biology, National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human Services, Research Triangle Park, North Carolina 27709, USA.

Nature Structural & Molecular Biology
|December 21, 2004
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

Persistence of large mtDNA rearrangements linked to premature aging in Pol γ exonuclease-deficient mice.

Nucleic acids research·2026
Same author

Reclassification of GST Allergens Based on Their Cross-Reactivity in Two Divergent Cockroach Species.

Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology·2026
Same author

Development of a specific and sensitive LC-MS/MS method to quantify Heparan Sulfate 3-O-Sulfotransferase-1 activity.

Glycobiology·2026
Same author

Evidence that MutSβ repairs indels generated by mispair initiated template slippage.

DNA repair·2026
Same author

Structural and Computational Analysis of <i>Pseudomonas aeruginosa</i> DNA Gyrase Reveals Molecular Characteristics That May Contribute to Ciprofloxacin Resistance.

Biomolecules·2026
Same author

A Human Monoclonal Antibody Displays Promiscuous Binding to Multiple Type 1 nsLTP Allergens.

Journal of investigational allergology & clinical immunology·2026
Same journal

Genome-wide absolute quantification of chromatin looping.

Nature structural & molecular biology·2026
Same journal

Putting numbers on chromatin looping.

Nature structural & molecular biology·2026
Same journal

Transcriptional readthrough progresses from incidental byproduct to therapeutic opportunity.

Nature structural & molecular biology·2026
Same journal

Distinct ATRX functions cooperate with 9-1-1 and CST complexes to safeguard replication and telomere integrity.

Nature structural & molecular biology·2026
Same journal

Structurally defining neurokinin selectivity to improve NK2R agonists.

Nature structural & molecular biology·2026
Same journal

Surveying the roles of NINJ1 in plasma membrane rupture.

Nature structural & molecular biology·2026
See all related articles

DNA polymerase lambda (Pol lambda) fills gaps in DNA repair. Crystal structures reveal Pol lambda

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • DNA repair mechanisms are crucial for maintaining genomic integrity.
  • Family X polymerases, including Pol lambda, are implicated in DNA repair pathways.
  • Understanding the catalytic mechanisms of DNA polymerases is essential for comprehending DNA replication and repair.

Purpose of the Study:

  • To elucidate the structural basis of Pol lambda's function in DNA repair.
  • To characterize the catalytic mechanism of Pol lambda at a single-nucleotide gap.
  • To investigate the conformational changes, if any, during Pol lambda-mediated nucleotide incorporation.

Main Methods:

  • X-ray crystallography was employed to determine the structures of Pol lambda.
  • Structures were captured at three distinct stages of single-nucleotide gap filling.

Related Experiment Videos

  • Analysis of the crystal structures focused on enzyme-substrate interactions and catalytic geometry.

    • Main Results:

    • Crystal structures of Pol lambda were obtained at three steps of single-nucleotide gap filling.
    • Pol lambda exhibits minimal subdomain movements during catalysis, distinguishing it from other DNA polymerases.
    • The study provides detailed insights into the in-line nucleotidyl transfer reaction's geometry and stereochemistry.

    Conclusions:

    • Pol lambda functions through a distinct catalytic mechanism involving limited conformational changes.
    • The structural data clarifies the precise geometric and stereochemical aspects of nucleotide addition by Pol lambda.
    • These findings enhance our understanding of DNA gap repair processes mediated by specialized polymerases.