SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase

Boris Pfander, George-Lucian Moldovan, Meik Sacher, Carsten Hoege and Stefan Jentsch ()
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Boris Pfander: Max Planck Institute of Biochemistry
George-Lucian Moldovan: Max Planck Institute of Biochemistry
Meik Sacher: Max Planck Institute of Biochemistry
Carsten Hoege: Max Planck Institute of Biochemistry
Stefan Jentsch: Max Planck Institute of Biochemistry

Nature, 2005, vol. 436, issue 7049, 428-433

Abstract: 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.

Date: 2005
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DOI: 10.1038/nature03665

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