Mte1 interacts with Mph1 and promotes crossover recombination
and telomere maintenance

J 2016

Mte1 interacts with Mph1 and promotes crossover recombination and telomere maintenance

SILVA, Sonia, Veronika ALTMANNOVÁ, Sarah LUKE-GLASER, Peter HENRIKSEN, Irene GALLINA et. al.

Basic information

Original name

Mte1 interacts with Mph1 and promotes crossover recombination and telomere maintenance

Authors

SILVA, Sonia (208 Denmark), Veronika ALTMANNOVÁ (203 Czech Republic, belonging to the institution), Sarah LUKE-GLASER (276 Germany), Peter HENRIKSEN (208 Denmark), Irene GALLINA (208 Denmark), Xuejiao YANG (208 Denmark), Chunaram CHOUDHARY (208 Denmark), Brian LUKE (276 Germany), Lumír KREJČÍ (203 Czech Republic, guarantor, belonging to the institution) and Michael LISBY (208 Denmark)

Edition

Genes & Development, Cold Spring Harbor, Cold Spring Harbor Laboratory Pres, 2016, 0890-9369

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

Genetics and molecular biology

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 9.413

RIV identification code

RIV/00216224:14110/16:00088199

Organization unit

Faculty of Medicine

DOI

http://dx.doi.org/10.1101/gad.276204.115

UT WoS

000371974500008

Keywords in English

homologous recombination; telomere maintenance; genome integrity; DNA repair; Mph1; Mte1

Abstract

V originále

Mph1 is a member of the conserved FANCM family of DNA motor proteins that play key roles in genome maintenance processes underlying Fanconi anemia, a cancer predisposition syndrome in humans. Here, we identify Mte1 as a novel interactor of the Mph1 helicase in Saccharomyces cerevisiae. In vitro, Mte1 (Mph1-associated telomere maintenance protein 1) binds directly to DNA with a preference for branched molecules such as D loops and fork structures. In addition, Mte1 stimulates the helicase and fork regression activities of Mph1 while inhibiting the ability of Mph1 to dissociate recombination intermediates. Deletion of MTE1 reduces crossover recombination and suppresses the sensitivity of mph1 Delta mutant cells to replication stress. Mph1 and Mte1 interdependently colocalize at DNA damage-induced foci and dysfunctional telomeres, and MTE1 deletion results in elongated telomeres. Taken together, our data indicate that Mte1 plays a role in regulation of crossover recombination, response to replication stress, and telomere maintenance.

Links

GAP207/12/2323, research and development project

Name: Endonuleazová a translokázová aktivita v restričních-modifikáčních komplexéch typu I

Investor: Czech Science Foundation

GA13-26629S, research and development project

Name: SUMO a stability genomu

Investor: Czech Science Foundation

ROZV/20/LF/2015, interní kód MU

Name: LF - Příspěvek IP 2015

Investor: Ministry of Education, Youth and Sports of the CR

Citovat

SILVA, Sonia, Veronika ALTMANNOVÁ, Sarah LUKE-GLASER, Peter HENRIKSEN, Irene GALLINA, Xuejiao YANG, Chunaram CHOUDHARY, Brian LUKE, Lumír KREJČÍ and Michael LISBY. Mte1 interacts with Mph1 and promotes crossover recombination and telomere maintenance. Genes & Development. Cold Spring Harbor: Cold Spring Harbor Laboratory Pres, 2016, vol. 30, No 6, p. 700-717. ISSN 0890-9369. Available from: https://dx.doi.org/10.1101/gad.276204.115.

@article{1355877,
   author = {Silva, Sonia and Altmannová, Veronika and LukeandGlaser, Sarah and Henriksen, Peter and Gallina, Irene and Yang, Xuejiao and Choudhary, Chunaram and Luke, Brian and Krejčí, Lumír and Lisby, Michael},
   article_location = {Cold Spring Harbor},
   article_number = {6},
   doi = {http://dx.doi.org/10.1101/gad.276204.115},
   keywords = {homologous recombination; telomere maintenance; genome integrity; DNA repair; Mph1; Mte1},
   language = {eng},
   issn = {0890-9369},
   journal = {Genes & Development},
   title = {Mte1 interacts with Mph1 and promotes crossover recombination and telomere maintenance},
   volume = {30},
   year = {2016}
}

TY  - JOUR
ID  - 1355877
AU  - Silva, Sonia - Altmannová, Veronika - Luke-Glaser, Sarah - Henriksen, Peter - Gallina, Irene - Yang, Xuejiao - Choudhary, Chunaram - Luke, Brian - Krejčí, Lumír - Lisby, Michael
PY  - 2016
TI  - Mte1 interacts with Mph1 and promotes crossover recombination and telomere maintenance
JF  - Genes & Development
VL  - 30
IS  - 6
SP  - 700-717
EP  - 700-717
PB  - Cold Spring Harbor Laboratory Pres
SN  - 08909369
KW  - homologous recombination
KW  - telomere maintenance
KW  - genome integrity
KW  - DNA repair
KW  - Mph1
KW  - Mte1
N2  - Mph1 is a member of the conserved FANCM family of DNA motor proteins that play key roles in genome maintenance processes underlying Fanconi anemia, a cancer predisposition syndrome in humans. Here, we identify Mte1 as a novel interactor of the Mph1 helicase in Saccharomyces cerevisiae. In vitro, Mte1 (Mph1-associated telomere maintenance protein 1) binds directly to DNA with a preference for branched molecules such as D loops and fork structures. In addition, Mte1 stimulates the helicase and fork regression activities of Mph1 while inhibiting the ability of Mph1 to dissociate recombination intermediates. Deletion of MTE1 reduces crossover recombination and suppresses the sensitivity of mph1 Delta mutant cells to replication stress. Mph1 and Mte1 interdependently colocalize at DNA damage-induced foci and dysfunctional telomeres, and MTE1 deletion results in elongated telomeres. Taken together, our data indicate that Mte1 plays a role in regulation of crossover recombination, response to replication stress, and telomere maintenance.
ER  -

SILVA, Sonia, Veronika ALTMANNOVÁ, Sarah LUKE-GLASER, Peter HENRIKSEN, Irene GALLINA, Xuejiao YANG, Chunaram CHOUDHARY, Brian LUKE, Lumír KREJČÍ and Michael LISBY. Mte1 interacts with Mph1 and promotes crossover recombination and telomere maintenance. \textit{Genes \&{} Development}. Cold Spring Harbor: Cold Spring Harbor Laboratory Pres, 2016, vol.~30, No~6, p.~700-717. ISSN~0890-9369. Available from: https://dx.doi.org/10.1101/gad.276204.115.

Detailed Information on Publication Record