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

The oligomeric T4 primase is the functional form during replication.

Jingsong Yang1, Jun Xi, Zhihao Zhuang

  • 1Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania 16802, USA.

The Journal of Biological Chemistry
|May 18, 2005
PubMed
Summary

Bacteriophage T4 primase (gp61) forms a functional hexamer, crucial for DNA replication. This oligomerization enhances priming activity and suggests a shared active site among subunits during lagging strand synthesis.

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

Food-derived antimicrobial peptides: advances in sources, mechanisms, structure-activity relationships, and AI-assisted design.

Food research international (Ottawa, Ont.)·2026
Same author

Introduction.

Advances in experimental medicine and biology·2026
Same author

Micro-aqueous hydration extraction for green and sustainable production of high-quality edible oils.

Food chemistry·2026
Same author

Impact of high-pressure steam on Ara h 3 antigenicity and the location of the sensitization disruption region.

Food chemistry·2026
Same author

Synergistic suppression of ammonia volatilization by biochar-compost through soil physicochemical and microbial regulation in saline-alkali soil.

Journal of environmental management·2026
Same author

Syntaxin1A in synaptopathies: From molecular mechanisms to therapeutic implications in neurological disorders (Review).

Biomedical reports·2026

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Virology

Background:

  • DNA primases synthesize RNA primers for DNA replication initiation.
  • In bacteriophage T4, primase (gp61) interacts with helicase (gp41) to form a primosome complex.
  • The hexameric nature of helicase (gp41) raises questions about primase (gp61) oligomeric structure.

Purpose of the Study:

  • To investigate the oligomeric state of bacteriophage T4 primase (gp61) during replication.
  • To determine if gp61 forms a hexameric structure, similar to its interacting helicase (gp41).
  • To elucidate the functional significance of gp61 oligomerization in DNA replication.

Main Methods:

  • Fluorescence anisotropy was used to determine primase/single-stranded DNA binding stoichiometry.

Related Experiment Videos

  • Enzyme kinetics, including measurement of the rate constant k(cat), were employed.
  • Hetero-oligomeric complementation assays using wild-type and mutant primases were performed.

    • Main Results:

    • Fluorescence anisotropy data suggested a 6:1 stoichiometry for primase binding.
    • Increased primase concentration correlated with a higher catalytic rate (k(cat)), indicating an oligomeric functional form.
    • Mixing inactive mutant primases with wild-type restored catalytic activity, confirming oligomerization and suggesting a shared active site.

    Conclusions:

    • The study provides strong evidence for the functional oligomerization of bacteriophage T4 primase (gp61).
    • gp61 likely forms a hexameric structure, contributing to efficient lagging strand DNA synthesis.
    • The findings suggest that gp61 oligomerization is essential for its enhanced priming activity.