Access
To read this story in full you will need to login or make a payment (see right).
Letter
Nature 436, 428-433 (21 July 2005) | doi:10.1038/nature03665; Received 29 November 2004; Accepted 15 April 2005; Published online 1 June 2005
Open Innovation Challenges
-
Fast Growth of Transformed Soybean Shoots
A method for accelerating growth of soybean shoots is desired.
-
Protect Enzyme from In Planta Degradation
A proposal for stable expression of an enzyme in corn seed is desired.
nature jobs
Principal Scientist for Pilot Plant - Solid Dosage Forms
- Novo Nordisk
- Bagsværd, Denmark
Laboratory Manager / Principal Research Assistant
- Wellcome Trust Sanger Institute
- Hinxton, Cambridge, CB10 1SA, UK
SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase
Boris Pfander1, George-Lucian Moldovan1, Meik Sacher1, Carsten Hoege1,2 & Stefan Jentsch1
- Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
- †Present address: Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01307 Dresden, Germany
Correspondence to: Stefan Jentsch1 Correspondence and requests for materials should be addressed to S.J. (Email: Jentsch@biochem.mpg.de).
Abstract
Damaged DNA, if not repaired before replication, can lead to replication fork stalling and genomic instability1, 2, 3; however, cells can switch to different damage bypass modes that permit replication across lesions. Two main bypasses are controlled by ubiquitin modification of proliferating cell nuclear antigen (PCNA), a homotrimeric DNA-encircling protein that functions as a polymerase processivity factor and regulator of replication-linked functions4, 5. Upon DNA damage, PCNA is modified at the conserved lysine residue 164 by either mono-ubiquitin or a lysine-63-linked multi-ubiquitin chain5, which induce error-prone or error-free replication bypasses of the lesions5, 6. In S phase, even in the absence of exogenous DNA damage, yeast PCNA can be alternatively modified by the small ubiquitin-related modifier protein SUMO5; however the consequences of this remain controversial5, 6, 7. Here we show by genetic analysis that SUMO-modified PCNA functionally cooperates with Srs2, a helicase that blocks recombinational repair by disrupting Rad51 nucleoprotein filaments8, 9. Moreover, Srs2 displays a preference for interacting directly with the SUMO-modified form of PCNA, owing to a specific binding site in its carboxy-terminal tail. Our finding suggests a model in which SUMO-modified PCNA recruits Srs2 in S phase in order to prevent unwanted recombination events of replicating chromosomes.
To read this story in full you will need to login or make a payment (see right).
MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated.
NEWS AND VIEWS
DNA repair Right on target with ubiquitinNature News and Views (12 Sep 2002)
Human therapeutic proteins from silkwormsNature Biotechnology Research News (01 Jan 2003)
See all 5 matches for News And ViewsRESEARCH
A GTP-binding adapter protein couples TRAIL receptors to apoptosis-inducing proteinsNature Immunology Article (01 Jun 2001)
A novel function of DNA polymerase ζ regulated by PCNAThe EMBO Journal Article (20 Sep 2006)
See all 59 matches for Research
