PMID- 28096179
OWN - NLM
STAT- MEDLINE
DCOM- 20170703
LR  - 20211204
IS  - 1460-2075 (Electronic)
IS  - 0261-4189 (Print)
IS  - 0261-4189 (Linking)
VI  - 36
IP  - 5
DP  - 2017 Mar 1
TI  - Dbf4-dependent kinase and the Rtt107 scaffold promote Mus81-Mms4 resolvase 
      activation during mitosis.
PG  - 664-678
LID - 10.15252/embj.201694831 [doi]
AB  - DNA repair by homologous recombination is under stringent cell cycle control. 
      This includes the last step of the reaction, disentanglement of DNA joint 
      molecules (JMs). Previous work has established that JM resolving nucleases are 
      activated specifically at the onset of mitosis. In case of budding yeast 
      Mus81-Mms4, this cell cycle stage-specific activation is known to depend on 
      phosphorylation by CDK and Cdc5 kinases. Here, we show that a third cell cycle 
      kinase, Cdc7-Dbf4 (DDK), targets Mus81-Mms4 in conjunction with Cdc5-both kinases 
      bind to as well as phosphorylate Mus81-Mms4 in an interdependent manner. 
      Moreover, DDK-mediated phosphorylation of Mms4 is strictly required for Mus81 
      activation in mitosis, establishing DDK as a novel regulator of homologous 
      recombination. The scaffold protein Rtt107, which binds the Mus81-Mms4 complex, 
      interacts with Cdc7 and thereby targets DDK and Cdc5 to the complex enabling full 
      Mus81 activation. Therefore, Mus81 activation in mitosis involves at least three 
      cell cycle kinases, CDK, Cdc5 and DDK Furthermore, tethering of the kinases in a 
      stable complex with Mus81 is critical for efficient JM resolution.
CI  - (c) 2017 The Authors. Published under the terms of the CC BY NC ND 4.0 license.
FAU - Princz, Lissa N
AU  - Princz LN
AD  - Max Planck Institute of Biochemistry, DNA Replication and Genome Integrity, 
      Martinsried, Germany.
FAU - Wild, Philipp
AU  - Wild P
AD  - Institute of Biochemistry, Eidgenossische Technische Hochschule, Zurich, 
      Switzerland.
FAU - Bittmann, Julia
AU  - Bittmann J
AD  - Max Planck Institute of Biochemistry, DNA Replication and Genome Integrity, 
      Martinsried, Germany.
FAU - Aguado, F Javier
AU  - Aguado FJ
AD  - Department of Biochemistry and Molecular Biology, Center for Research in 
      Molecular Medicine and Chronic Diseases, Universidade de Santiago de Compostela, 
      Santiago de Compostela, Spain.
FAU - Blanco, Miguel G
AU  - Blanco MG
AUID- ORCID: 0000-0002-2883-7326
AD  - Department of Biochemistry and Molecular Biology, Center for Research in 
      Molecular Medicine and Chronic Diseases, Universidade de Santiago de Compostela, 
      Santiago de Compostela, Spain.
FAU - Matos, Joao
AU  - Matos J
AD  - Institute of Biochemistry, Eidgenossische Technische Hochschule, Zurich, 
      Switzerland.
FAU - Pfander, Boris
AU  - Pfander B
AUID- ORCID: 0000-0003-2180-5054
AD  - Max Planck Institute of Biochemistry, DNA Replication and Genome Integrity, 
      Martinsried, Germany bpfander@biochem.mpg.de.
LA  - eng
PT  - Journal Article
DEP - 20170117
PL  - England
TA  - EMBO J
JT  - The EMBO journal
JID - 8208664
RN  - 0 (Cell Cycle Proteins)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Nuclear Proteins)
RN  - 0 (RTT107 protein, S cerevisiae)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - EC 2.7.1.- (CDC7 protein, S cerevisiae)
RN  - EC 2.7.11.1 (Protein Serine-Threonine Kinases)
RN  - EC 2.7.11.21 (CDC5 protein, S cerevisiae)
RN  - EC 3.1.- (Endonucleases)
RN  - EC 3.1.- (Flap Endonucleases)
RN  - EC 3.1.- (MUS81 protein, S cerevisiae)
RN  - EC 3.1.22.- (MMS4 protein, S cerevisiae)
SB  - IM
MH  - Cell Cycle Proteins/*metabolism
MH  - DNA-Binding Proteins/*metabolism
MH  - Endonucleases/*metabolism
MH  - Enzyme Activation
MH  - Flap Endonucleases/*metabolism
MH  - *Mitosis
MH  - Nuclear Proteins/*metabolism
MH  - Protein Serine-Threonine Kinases/*metabolism
MH  - Saccharomyces cerevisiae/enzymology/*physiology
MH  - Saccharomyces cerevisiae Proteins/*metabolism
PMC - PMC5331752
OTO - NOTNLM
OT  - cell cycle
OT  - genome stability
OT  - homologous recombination
OT  - joint molecule resolution
OT  - post-translational modification
EDAT- 2017/01/18 06:00
MHDA- 2017/07/04 06:00
PMCR- 2017/01/17
CRDT- 2017/01/19 06:00
PHST- 2016/05/22 00:00 [received]
PHST- 2016/12/15 00:00 [revised]
PHST- 2016/12/19 00:00 [accepted]
PHST- 2017/01/18 06:00 [pubmed]
PHST- 2017/07/04 06:00 [medline]
PHST- 2017/01/19 06:00 [entrez]
PHST- 2017/01/17 00:00 [pmc-release]
AID - embj.201694831 [pii]
AID - EMBJ201694831 [pii]
AID - 10.15252/embj.201694831 [doi]
PST - ppublish
SO  - EMBO J. 2017 Mar 1;36(5):664-678. doi: 10.15252/embj.201694831. Epub 2017 Jan 17.