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

Potential double-flipping mechanism by E. coli MutY.

P G House1, D E Volk, V Thiviyanathan

  • 1Center for Molecular Science, University of Texas Medical Branch, Galveston, Texas 77555-1071, USA.

Progress in Nucleic Acid Research and Molecular Biology
|September 14, 2001
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

How to integrate atopic dermatitis in the management of skin neglected tropical diseases in Sub-Saharan Africa?

Journal of the European Academy of Dermatology and Venereology : JEADV·2023
Same author

A prospective investigation to evaluate risk factors for lower extremity injury risk in male youth soccer players.

Scandinavian journal of medicine & science in sports·2017
Same author

Differential inflammasome activation signatures following intracellular infection of human macrophages with Mycobacterium bovis BCG or Trypanosoma cruzi.

Tuberculosis (Edinburgh, Scotland)·2016
Same author

Structures of Thymosin Proteins.

Vitamins and hormones·2016
Same author

Medical co-morbidities of patients with haemophilia: pain, obesity and hepatitis C.

Haemophilia : the official journal of the World Federation of Hemophilia·2016
Same author

In vivo targeting of leukemia stem cells by directing parthenolide-loaded nanoparticles to the bone marrow niche.

Leukemia·2015

The DNA repair glycosylase MutY recognizes and removes mismatched bases in DNA. Structural and functional analyses reveal MutY

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • MutY is a DNA repair glycosylase essential for removing specific mismatched bases in double-stranded DNA.
  • Understanding MutY's structure is crucial for elucidating its DNA repair mechanisms.
  • Previous attempts to determine the intact MutY structure were unsuccessful.

Purpose of the Study:

  • To determine the structural basis for MutY's recognition and removal of mismatched DNA bases.
  • To elucidate the catalytic mechanism and substrate specificity of MutY.

Main Methods:

  • Limited proteolytic digestion to obtain functional domains.
  • X-ray crystallography to determine the structure of the 26-kDa catalytic domain (p26MutY).
  • NMR spectroscopy to solve the solution structure of the 13-kDa noncatalytic domain.

Related Experiment Videos

  • Molecular modeling to integrate MutY domains with DNA.

    • Main Results:

    • MutY comprises a 26-kDa catalytic domain (p26MutY) and a 13-kDa domain involved in specificity.
    • X-ray structures of p26MutY revealed its catalytic mechanism, including adenine binding.
    • NMR structure of the 13-kDa domain shows similarity to MutT, a pyrophosphohydrolase.
    • Molecular modeling suggests MutY wraps DNA and flips bases like adenine and 8-oxoguanine for repair.

    Conclusions:

    • MutY functions through distinct catalytic and specificity domains.
    • The enzyme likely initiates repair by extruding mismatched bases from the DNA helix.
    • Structural insights provide a foundation for understanding MutY-mediated DNA repair pathways.