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  A cell cycle-regulated Slx4-Dpb11 complex promotes the resolution of DNA repair intermediates linked to stalled replication

Gritenaite, D., Princz, L., Szakal, B., Bantele, S. C. S., Wendeler, L., Schilbach, S., et al. (2014). A cell cycle-regulated Slx4-Dpb11 complex promotes the resolution of DNA repair intermediates linked to stalled replication. GENES & DEVELOPMENT, 28(14), 1604-1619. doi:10.1101/gad.240515.114.

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 Creators:
Gritenaite, Dalia1, Author              
Princz, Lissa1, Author              
Szakal, Barnabas2, Author
Bantele, Susanne C. S.1, Author              
Wendeler, Lina1, Author              
Schilbach, Sandra1, Author              
Habermann, Bianca3, Author              
Matos, Joao2, Author
Lisby, Michael2, Author
Branzei, Dana2, Author
Pfander, Boris1, Author              
Affiliations:
1Pfander, Boris / DNA Replication and Genome Integrity, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565165              
2external, ou_persistent22              
3Habermann, Bianca / Computational Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1832284              

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Free keywords: STRUCTURE-SPECIFIC NUCLEASES; HOLLIDAY JUNCTION RESOLVASE; BUDDING YEAST; DAMAGE CHECKPOINT; S-PHASE; SACCHAROMYCES-CEREVISIAE; ANAPHASE BRIDGES; PHOSPHORYLATION; RECOMBINATION; DPB11DNA damage response; cell cycle; post-replicative repair; homologous recombination; joint molecule resolution;
 Abstract: A key function of the cellular DNA damage response is to facilitate the bypass of replication fork-stalling DNA lesions. Template switch reactions allow such a bypass and involve the formation of DNA joint molecules (JMs) between sister chromatids. These JMs need to be resolved before cell division; however, the regulation of this process is only poorly understood. Here, we identify a regulatory mechanism in yeast that critically controls JM resolution by the Mus81-Mms4 endonuclease. Central to this regulation is a conserved complex comprising the scaffold proteins Dpb11 and Slx4 that is under stringent control. Cell cycle-dependent phosphorylation of Slx4 by Cdk1 promotes the Dpb11-Slx4 interaction, while in mitosis, phosphorylation of Mms4 by Polo-like kinase Cdc5 promotes the additional association of Mus81-Mms4 with the complex, thereby promoting JM resolution. Finally, the DNA damage checkpoint counteracts Mus81-Mms4 binding to the Dpb11-Slx4 complex. Thus, Dpb11-Slx4 integrates several cellular inputs and participates in the temporal program for activation of the JM-resolving nuclease Mus81.

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Language(s): eng - English
 Dates: 2014
 Publication Status: Published in print
 Pages: 16
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000339166100009
DOI: 10.1101/gad.240515.114
 Degree: -

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Title: GENES & DEVELOPMENT
Source Genre: Journal
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Publ. Info: 1 BUNGTOWN RD, COLD SPRING HARBOR, NY 11724 USA : COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
Pages: - Volume / Issue: 28 (14) Sequence Number: - Start / End Page: 1604 - 1619 Identifier: ISSN: 0890-9369