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

PCNASUMO and Srs2: a model SUMO substrate-effector pair.

H D Ulrich1

  • 1Cancer Research UK, Clare Hall Laboratories, London Research Institute, South Mimms EN6 3LD, U.K. helle.ulrich@cancer.org.uk

Biochemical Society Transactions
|November 23, 2007
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

RAD18, WRNIP1 and ATMIN promote ATM signalling in response to replication stress.

Oncogene·2016
Same author

RAD18, WRNIP1 and ATMIN promote ATM signalling in response to replication stress.

Oncogene·2015
Same author

Conservation of DNA damage tolerance pathways from yeast to humans.

Biochemical Society transactions·2007
Same author

A prokaryotic condensin/cohesin-like complex can actively compact chromosomes from a single position on the nucleoid and binds to DNA as a ring-like structure.

Molecular and cellular biology·2003
Same author

Natural substrates of the proteasome and their recognition by the ubiquitin system.

Current topics in microbiology and immunology·2002
Same author

The srs2 suppressor of UV sensitivity acts specifically on the RAD5- and MMS2-dependent branch of the RAD6 pathway.

Nucleic acids research·2001
Same journal

TDP-43 proteinopathy as a biomarker and therapeutic target in amyotrophic lateral sclerosis.

Biochemical Society transactions·2026
Same journal

Advancing the monitoring of organelle contact sites in vitro and in vivo.

Biochemical Society transactions·2026
Same journal

Mechanisms influencing transient cytoplasmic protein targeting to intracellular lipid droplets.

Biochemical Society transactions·2026
Same journal

Replication associated nuclear DNA mismatch repair across kingdoms.

Biochemical Society transactions·2026
Same journal

Phosphatases of regenerating liver downregulate PTEN to promote tumorigenesis.

Biochemical Society transactions·2026
Same journal

Implications of Rho GTPase signaling in cancer immunotherapy.

Biochemical Society transactions·2026
See all related articles

SUMOylation of PCNA in yeast recruits the Srs2 helicase to replication forks, preventing unwanted recombination. This SUMOylation mechanism highlights how SUMOylation regulates target proteins and activates downstream effectors.

Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • SUMOylation (small ubiquitin-related modifier) is a post-translational modification that regulates protein function.
  • Proliferating Cell Nuclear Antigen (PCNA) is a key factor in DNA replication.
  • Unscheduled recombination can lead to genomic instability.

Purpose of the Study:

  • To review the mechanism by which SUMOylation of PCNA recruits the Srs2 helicase.
  • To discuss how this interaction prevents unscheduled recombination events.
  • To illustrate how SUMOylation modulates target protein properties and activates downstream effectors.

Main Methods:

  • Literature review of studies on SUMOylation, PCNA, and Srs2 in budding yeast.
  • Analysis of the interaction between SUMOylated PCNA and Srs2.

Related Experiment Videos

  • Discussion of the functional consequences of this interaction.

    • Main Results:

    • SUMOylation of PCNA recruits the Srs2 helicase to active replication forks.
    • This recruitment prevents unscheduled recombination events during DNA replication.
    • The SUMOylation-PCNA-Srs2 interaction serves as a model for SUMOylation-mediated regulation.

    Conclusions:

    • SUMOylation of PCNA is a critical mechanism for maintaining genome stability by preventing recombination.
    • The interaction between SUMOylated PCNA and Srs2 exemplifies how SUMOylation controls protein function and downstream signaling.
    • This regulatory pathway is essential for proper DNA replication and cellular integrity.