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MRE11 meiotic recombination 11 homolog A

Mre11
This gene encodes a nuclear protein involved in homologous recombination, telomere length maintenance, and DNA double-strand break repair. By itself, the protein has 3' to 5' exonuclease activity and endonuclease activity. The protein forms a complex with the RAD50 homolog; this complex is required for nonhomologous joining of DNA ends and possesses increased single-stranded DNA endonuclease and 3' to 5' exonuclease activities. In conjunction with a DNA ligase, this protein promotes the joining of noncomplementary ends in vitro using short homologies near the ends of the DNA fragments. This gene has a pseudogene on chromosome 3. Alternative splicing of this gene results in two transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Rad50, NBS1, Atm, CAN, Rad51
Papers on Mre11
Yeast MRX deletions have short chronological life span and more triacylglycerols.
New
Srinivasan et al., Mysore, India. In Fems Yeast Res, Feb 2016
Among these, RAD50, MRE11 and XRS2 form a complex, MRX that is involved in homologous recombination that showed an increase in the amount of TAG.
Microhomology-mediated end joining is the principal mediator of double-strand break repair during mitochondrial DNA lesions.
New
Raghavan et al., Bengaluru, India. In Mol Biol Cell, Feb 2016
Western blotting, immunoprecipitation, and protein inhibition assays suggest the involvement of CtIP, FEN1, MRE11, and PARP1 in mitochondrial MMEJ.
DNA damage response during mouse oocyte maturation.
New
Solc et al., Australia. In Cell Cycle, Feb 2016
MRE11, but not ATM, is essential to detect DSBs in prophase I and is involved in H2AX phosphorylation during metaphase I. Inhibiting MRE11 by mirin during meiotic maturation results in anaphase bridges and also increases the number of γH2AX foci in metaphase II.
S. cerevisiae Mre11 recruits conjugated SUMO moieties to facilitate the assembly and function of the Mre11-Rad50-Xrs2 complex.
New
Wang et al., Taipei, Taiwan. In Nucleic Acids Res, Feb 2016
The yeast and mammalian Mre11-Rad50-Xrs2/Nbs1 (MRX/N)-Sae2/Ctp1 complex catalyzes the resection of DSBs induced by secondary structures, chemical adducts or covalently-attached proteins.
Expression of DNA double-strand break repair proteins predicts the response and prognosis of colorectal cancer patients undergoing oxaliplatin-based chemotherapy.
New
Kato et al., Mibu, Japan. In Oncol Rep, Jan 2016
The expression of DSB repair proteins such as RAD51 and MRE11 was investigated by immunohistochemistry, and associations between RAD51 and MRE11 expression and clinicopathological factors or chemotherapeutic effect were assessed.
Chromatin perturbations during the DNA damage response in higher eukaryotes.
Review
New
Kastan et al., Pittsburgh, United States. In Dna Repair (amst), Dec 2015
The MRE11-RAD50-NBS1 (MRN) complex, which has a catalytic role in DNA repair, and the KAT5 (Tip60) acetyltransferase are required for maximal ATM kinase activation in cells exposed to low doses of ionizing radiation.
Mechanisms of Origin, Phenotypic Effects and Diagnostic Implications of Complex Chromosome Rearrangements.
Review
New
Haaf et al., Würzburg, Germany. In Mol Syndromol, Sep 2015
Therefore, the putative functions of the proteins encoded by ATM, BLM, WRN, ATR, MRE11, NBS1, and RAD51 in preventing CCRs are discussed.
Viral and Cellular Genomes Activate Distinct DNA Damage Responses.
New
Impact
O'Shea et al., Los Angeles, United States. In Cell, Sep 2015
In response to cellular genome breaks, MRE11/RAD50/NBS1 (MRN) activates a global ATM DNA damage response (DDR) that prevents cellular replication.
DNA damage foci: Meaning and significance.
Review
New
Burdak-Rothkamm et al., United Kingdom. In Environ Mol Mutagen, Jul 2015
The discovery of DNA damage response proteins such as γH2AX, ATM, 53BP1, RAD51, and the MRE11/RAD50/NBS1 complex, that accumulate and/or are modified in the vicinity of a chromosomal DNA double-strand break to form microscopically visible, subnuclear foci, has revolutionized the detection of these lesions and has enabled studies of the cellular machinery that contributes to their repair.
Hsp90: A New Player in DNA Repair?
Review
di Masi et al., Roma, Italy. In Biomolecules, 2014
Multiple components of the DNA double strand breaks repair machinery, including BRCA1, BRCA2, CHK1, DNA-PKcs, FANCA, and the MRE11/RAD50/NBN complex, have been described to be client proteins of Hsp90, which acts as a regulator of the diverse DDR pathways.
Functional Role of NBS1 in Radiation Damage Response and Translesion DNA Synthesis.
Review
Komatsu et al., Kyoto, Japan. In Biomolecules, 2014
The C-terminus of NBS1 is essential for interactions with MRE11, a homologous recombination repair nuclease, and ATM, a key player in signal transduction after the generation of DNA double-strand breaks (DSBs), which is induced by IR.
A structural basis for the assembly and functions of a viral polymer that inactivates multiple tumor suppressors.
Impact
O'Shea et al., Los Angeles, United States. In Cell, 2012
E4-ORF3 forms a nuclear polymer and simultaneously inactivates p53, PML, TRIM24, and MRE11/RAD50/NBS1 (MRN) tumor suppressors.
Adenovirus regulates sumoylation of Mre11-Rad50-Nbs1 components through a paralog-specific mechanism.
GeneRIF
Hearing et al., Stony Brook, United States. In J Virol, 2012
Mre11 and Nbs1 are sumoylated during Ad5 infection and the E4-ORF3 protein is necessary and sufficient to induce SUMO conjugation. Relocalization of Mre11 and Nbs1 into E4-ORF3 nuclear tracks is required for this modification to occur.
Site-specific DICER and DROSHA RNA products control the DNA-damage response.
Impact
d'Adda di Fagagna et al., Milano, Italy. In Nature, 2012
Through RNA deep sequencing and the study of DDR activation at a single inducible DNA double-strand break, we demonstrate that DDR foci formation requires site-specific DICER- and DROSHA-dependent small RNAs, named DDRNAs, which act in a MRE11–RAD50–NBS1-complex-dependent manner (MRE11 also known as MRE11A; NBS1 also known as NBN).
Exome capture reveals ZNF423 and CEP164 mutations, linking renal ciliopathies to DNA damage response signaling.
Impact
GeneRIF
Hildebrandt et al., Ann Arbor, United States. In Cell, 2012
Study identifies by whole-exome resequencing, mutations of MRE11, ZNF423, and CEP164 as causing Nephronophthisis-related ciliopathies.
Mre11-dependent degradation of stalled DNA replication forks is prevented by BRCA2 and PARP1.
GeneRIF
Helleday et al., Oxford, United Kingdom. In Cancer Res, 2012
findings not only show that Mre11 activity is required for the survival of BRCA2 mutant cells but also elucidate roles for both the BRCA2 and PARP1 proteins in protecting stalled replication forks
Human Ku70/80 protein blocks exonuclease 1-mediated DNA resection in the presence of human Mre11 or Mre11/Rad50 protein complex.
GeneRIF
Chen et al., Dallas, United States. In J Biol Chem, 2012
Human Ku70/80 protein blocks exonuclease 1-mediated DNA resection in the presence of human Mre11 or Mre11/Rad50 protein complex.
Mre11 regulates CtIP-dependent double-strand break repair by interaction with CDK2.
GeneRIF
Ferguson et al., Ann Arbor, United States. In Nat Struct Mol Biol, 2012
The authors show that, in human and mouse, Mre11 controls these events through a direct interaction with CDK2 that is required for CtIP phosphorylation and BRCA1 interaction in normally dividing cells.
Double-strand break repair-independent role for BRCA2 in blocking stalled replication fork degradation by MRE11.
Impact
GeneRIF
Jasin et al., New York City, United States. In Cell, 2011
BRCA2 prevents chromosomal aberrations on replication stalling, which are alleviated by inhibition of MRE11, the nuclease responsible for this form of fork instability.
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