Source:http://linkedlifedata.com/resource/pubmed/id/15931174
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
7049
|
| pubmed:dateCreated |
2005-7-21
|
| pubmed:abstractText |
Damaged DNA, if not repaired before replication, can lead to replication fork stalling and genomic instability; 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 functions. Upon DNA damage, PCNA is modified at the conserved lysine residue 164 by either mono-ubiquitin or a lysine-63-linked multi-ubiquitin chain, which induce error-prone or error-free replication bypasses of the lesions. In S phase, even in the absence of exogenous DNA damage, yeast PCNA can be alternatively modified by the small ubiquitin-related modifier protein SUMO; however the consequences of this remain controversial. Here we show by genetic analysis that SUMO-modified PCNA functionally cooperates with Srs2, a helicase that blocks recombinational repair by disrupting Rad51 nucleoprotein filaments. 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.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/HPR5 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Proliferating Cell Nuclear Antigen,
http://linkedlifedata.com/resource/pubmed/chemical/RAD6 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/SUMO-1 Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Conjugating Enzymes
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
1476-4687
|
| pubmed:author | |
| pubmed:issnType |
Electronic
|
| pubmed:day |
21
|
| pubmed:volume |
436
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
428-33
|
| pubmed:dateRevised |
2009-6-17
|
| pubmed:meshHeading |
pubmed-meshheading:15931174-Chromosomes, Fungal,
pubmed-meshheading:15931174-DNA Damage,
pubmed-meshheading:15931174-DNA Helicases,
pubmed-meshheading:15931174-DNA Replication,
pubmed-meshheading:15931174-Epistasis, Genetic,
pubmed-meshheading:15931174-Mutagenesis,
pubmed-meshheading:15931174-Mutation,
pubmed-meshheading:15931174-Phenotype,
pubmed-meshheading:15931174-Proliferating Cell Nuclear Antigen,
pubmed-meshheading:15931174-Protein Binding,
pubmed-meshheading:15931174-Recombination, Genetic,
pubmed-meshheading:15931174-S Phase,
pubmed-meshheading:15931174-SUMO-1 Protein,
pubmed-meshheading:15931174-Saccharomyces cerevisiae,
pubmed-meshheading:15931174-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:15931174-Sequence Homology, Nucleic Acid,
pubmed-meshheading:15931174-Substrate Specificity,
pubmed-meshheading:15931174-Ubiquitin-Conjugating Enzymes
|
| pubmed:year |
2005
|
| pubmed:articleTitle |
SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase.
|
| pubmed:affiliation |
Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|