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

cDNAs encoding the large subunit of human replication factor C

F Bunz1, R Kobayashi, B Stillman

  • 1Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724.

Proceedings of the National Academy of Sciences of the United States of America
|December 1, 1993
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

Evolution of DNA replication origin specification and gene silencing mechanisms.

Nature communications·2020
Same author

Point prevalence survey for tick-borne pathogens in military working dogs, shelter animals, and pet populations in northern Colombia.

Journal of special operations medicine : a peer reviewed journal for SOF medical professionals·2014
Same author

Computer-based video analysis of movement.

The Australian journal of physiotherapy·2014
Same author

Perceptions of the clinical efficacy of laser therapy.

The Australian journal of physiotherapy·2014
Same author

ATR mediates cisplatin resistance in a p53 genotype-specific manner.

Oncogene·2011
Same author

Human cancer cells require ATR for cell cycle progression following exposure to ionizing radiation.

Oncogene·2006
Same journal

The TaMYB55-TaSnRK1α1-TabZIP9 module confers heat stress tolerance in wheat.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Superstatistics approach to turbulent circulation fluctuations.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

A molecular timescale for evolution of cobamide biosynthesis.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Pierre Chambon, a pioneer of molecular biology and gene regulation in eukaryotes.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Granulosa cell glycogen fuels the avascular corpus luteum.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Synthetic essentiality of TRAIL/TNFSF10 in VHL-deficient renal cell carcinoma.

Proceedings of the National Academy of Sciences of the United States of America·2026
See all related articles

Replication factor C (RFC) is crucial for DNA synthesis. This study isolated and analyzed cDNAs encoding a key RFC subunit, revealing conserved motifs and similarities to other DNA-binding proteins.

Area of Science:

  • Molecular Biology
  • Virology
  • Biochemistry

Background:

  • Replication factor C (RFC) is a vital DNA polymerase accessory protein for DNA replication.
  • RFC functions as a DNA-dependent ATPase, binding specifically to primer-template junctions.

Purpose of the Study:

  • To isolate and analyze cDNAs encoding the 140-kDa subunit of Replication factor C.
  • To characterize the molecular properties of this RFC subunit.

Main Methods:

  • cDNA isolation and sequencing.
  • Bioinformatic analysis of the coding sequence and predicted protein.

Main Results:

  • A 3.4 kb open reading frame was identified, encoding an 1148-amino acid protein (130 kDa).
  • The protein contains a putative ATP-binding motif and a conserved "DEAD" box.

Related Experiment Videos

  • Significant sequence identity was found with a murine DNA-binding protein and similarities with poly(ADP-ribose) polymerase and bacterial DNA ligases.

    • Conclusions:

    • The identified cDNAs encode a key subunit of Replication factor C.
    • Conserved motifs suggest functional roles in ATP binding and DNA interaction.
    • Structural similarities indicate potential shared mechanisms with other DNA-binding and ligating enzymes.