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

Crystal structure of a replication fork single-stranded DNA binding protein (T4 gp32) complexed to DNA

Y Shamoo1, A M Friedman, M R Parsons

  • 1Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520-8114, USA.

Nature
|July 27, 1995
PubMed
Summary

The bacteriophage T4 gp32 protein binds single-stranded DNA (ssDNA) to ensure DNA replication, repair, and recombination. Its crystal structure reveals how gp32 acts as a chaperone, facilitating DNA strand movement.

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

Outcomes during delivery hospitalisations with inflammatory bowel disease.

BJOG : an international journal of obstetrics and gynaecology·2022
Same author

Population risk factors for nulliparous, term, singleton, vertex caesarean birth: a national cross-sectional study.

BJOG : an international journal of obstetrics and gynaecology·2021
Same author

Inferring risk from a common drug exposure in pregnancy.

BJOG : an international journal of obstetrics and gynaecology·2019
Same author

Impact of timing of delivery on maternal and neonatal outcomes for women after three previous caesarean deliveries; a secondary analysis of the caesarean section registry.

BJOG : an international journal of obstetrics and gynaecology·2019
Same author

Which risk factors for thromboembolism should guide obstetric prophylaxis?

BJOG : an international journal of obstetrics and gynaecology·2018
Same author

Pathogenic Nocardia cyriacigeorgica and Nocardia nova Evolve To Resist Trimethoprim-Sulfamethoxazole by both Expected and Unexpected Pathways.

Antimicrobial agents and chemotherapy·2018

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Virology

Background:

  • The single-stranded DNA (ssDNA) binding protein gp32 is crucial for bacteriophage T4 DNA replication, recombination, and repair.
  • In vivo, gp32 binds ssDNA at the replication fork, enhancing replisome processivity and accuracy significantly.

Purpose of the Study:

  • To determine the crystal structure of the gp32 DNA binding domain complexed with ssDNA.
  • To elucidate the molecular mechanisms by which gp32 interacts with and modulates ssDNA dynamics.

Main Methods:

  • X-ray crystallography was used to determine the structure of the gp32 ssDNA complex at 2.2 Å resolution.

Main Results:

  • The crystal structure revealed an ssDNA binding cleft formed by three subdomains, featuring a positively charged surface and hydrophobic pockets.

Related Experiment Videos

  • Weak electron density for ssDNA suggests significant mobility, with the phosphate backbone interacting with the protein's electropositive cleft and bases contacting hydrophobic pockets.

    • Conclusions:

    • Gp32 functions as a sequence-independent ssDNA chaperone, enabling the largely unstructured ssDNA to slide through its binding cleft.
    • The structural data provides insights into gp32's roles in DNA metabolism, including template configuration, secondary structure melting, nuclease protection, and homologous recombination facilitation.