YEAST:MRE11

Species (Taxon ID)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s)	MRE11
Protein Name(s)	Double-strand break repair protein MRE11
External Links
UniProt	P32829
EMBL	D11463 Z49939 U60829 BK006946
PIR	S57592
RefSeq	NP_013951.1
ProteinModelPortal	P32829
SMR	P32829
BioGrid	35402
DIP	DIP-1313N
IntAct	P32829
MINT	MINT-388080
MaxQB	P32829
PaxDb	P32829
EnsemblFungi	[example_ID YMR224C]
GeneID	855264
KEGG	sce:YMR224C
CYGD	YMR224c
SGD	S000004837
eggNOG	COG0420
GeneTree	ENSGT00390000017288
HOGENOM	HOG000216581
InParanoid	P32829
KO	K10865
OMA	RMFVNKQ
OrthoDB	EOG7J187V
BioCyc	YEAST:G3O-32905-MONOMER
Reactome	REACT_243677 REACT_268498
NextBio	978864
PRO	PR:P32829
Proteomes	UP000002311
Genevestigator	P32829
GO	GO:0030870 GO:0005654 GO:0005634 GO:0008408 GO:0008296 GO:0003691 GO:0004520 GO:0004519 GO:0051880 GO:0030145 GO:0032947 GO:0043047 GO:0042162 GO:0030437 GO:0006284 GO:0000737 GO:0010791 GO:0006281 GO:0000727 GO:0006303 GO:0042138 GO:0000706 GO:0097552 GO:0046939 GO:0007131 GO:0051037
Gene3D	3.60.21.10
InterPro	IPR004843 IPR003701 IPR029052 IPR007281
PANTHER	PTHR10139
Pfam	PF00149 PF04152
PIRSF	PIRSF000882
SUPFAM	SSF56300
TIGRFAMs	TIGR00583

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0007126	meiosis	PMID:9858579^[1]	ECO:0000315			P	Figure 8	complete CACAO 2020
	GO:0010780	meiotic DNA double-strand break formation involved in reciprocal meiotic recombination	PMID:7625279^[2]	ECO:0000315			P	Table 1	complete CACAO 5031
	GO:0042138	meiotic DNA double-strand break formation	PMID:7625279^[2]	ECO:0000315			P	Table 1	complete CACAO 5032
	GO:0030437	ascospore formation	PMID:7625279^[2]	ECO:0000315			P	See Table 1	complete CACAO 5039
	GO:0006302	double-strand break repair	PMID:22002605^[3]	ECO:0000315			P	Figure 1 To investigate a specific role for the Mre11 3′–5′ exonuclease during DNA repair in cycling cells, we challenged yeast cells with exposure to DNA damaging agents. Similar to complete abrogation of the endo/exonuclease activities (mre11-H125N), reduced Mre11 exonuclease activity (mre11-H59S) sensitized cells to the DNA alkylating agent methyl methanesulphonate (MMS) and to the topoisomerase poison camptothecin (CPT; Fig. 3).Compared to an MRE11 deletion, however, mre11-H59S and mre11-H125N are themselves far less sensitive, consistent with physical interactions within the Mre11 complex being retained (Supplementary Fig. 9). In agreement with Mre11 endonuclease activity being unaffected in mre11-H59S, and allowing redundant processing pathways, combining mre11-H59S with a deletion of EXO1 did not further sensitize cells to MMS (Supplementary Fig. 10). Together these observations indicate that the exonuclease activity of Mre11 is involved in the repair of various classes of DNA lesion.	complete CACAO 5537
	GO:0010780	meiotic DNA double-strand break formation involved in reciprocal meiotic recombination	PMID:7625279^[2]	ECO:0000315			P	Table 1	complete CACAO 5137
	GO:0008296	3'-5'-exodeoxyribonuclease activity	PMID:22002605^[3]	ECO:0000315			F	Figure 2C shows that Mre11 has 3'-5' exonuclease activity on DNA, and that the mutant Mre-11 (H59S) has it to a lesser degree.	complete CACAO 5659
	GO:0030870	Mre11 complex	PMID:27746018^[4]	ECO:0000314			C	Fig 4C: C) Recombinant Mre11-Rad50 (MR) and Mre11-Rad50-Xrs2 (MRX) used in this study. Saccharomyces cerevisiae MRE11.	complete CACAO 12786
part_of	GO:0005739	mitochondrion	PMID:16823961^[5]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:22842922^[6]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:14576278^[7]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0035753	maintenance of DNA trinucleotide repeats	PMID:27173583^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0000723	telomere maintenance	PMID:9501103^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006303	double-strand break repair via nonhomologous end joining	PMID:9501103^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0008296	3'-5'-exodeoxyribonuclease activity	PMID:22002605^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006302	double-strand break repair	PMID:22002605^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0030437	ascospore formation	PMID:7625279^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0010780	meiotic DNA double-strand break formation involved in reciprocal meiotic recombination	PMID:7625279^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0010791	DNA double-strand break processing involved in repair via synthesis-dependent strand annealing	PMID:23254329^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0097552	mitochondrial double-strand break repair via homologous recombination	PMID:22214610^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0051880	G-quadruplex DNA binding	PMID:17698079^[12]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0051037	regulation of transcription involved in meiotic cell cycle	PMID:17396017^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0043047	single-stranded telomeric DNA binding	PMID:17698079^[12]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0042162	telomeric DNA binding	PMID:16116037^[14]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0042162	telomeric DNA binding	PMID:15721260^[15]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0032947	protein-containing complex scaffold activity	PMID:9845372^[16]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000002777 SGD:S000005194	F	Seeded From UniProt	complete
enables	GO:0032947	protein-containing complex scaffold activity	PMID:9845372^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0030870	Mre11 complex	PMID:9845372^[16]	ECO:0000353	physical interaction evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0030437	ascospore formation	PMID:17396017^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0008408	3'-5' exonuclease activity	PMID:11454871^[17]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0007131	reciprocal meiotic recombination	PMID:8417989^[18]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006303	double-strand break repair via nonhomologous end joining	PMID:12399380^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006284	base-excision repair	PMID:20040573^[20]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	PMID:7789757^[21]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:9845372^[16]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:15548595^[22]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0004520	endodeoxyribonuclease activity	PMID:16116037^[14]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004519	endonuclease activity	PMID:9858579^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
contributes_to	GO:0004017	adenylate kinase activity	PMID:17349953^[23]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003691	double-stranded telomeric DNA binding	PMID:17698079^[12]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0000727	double-strand break repair via break-induced replication	PMID:17321803^[24]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000004897	P	Seeded From UniProt	complete
involved_in	GO:0000727	double-strand break repair via break-induced replication	PMID:17321803^[24]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0097552	mitochondrial double-strand break repair via homologous recombination	PMID:21873635^[25]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000015644 SGD:S000004837	P	Seeded From UniProt	complete
involved_in	GO:0042138	meiotic DNA double-strand break formation	PMID:21873635^[25]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000015644 PomBase:SPAC13C5.07	P	Seeded From UniProt	complete
involved_in	GO:0031573	intra-S DNA damage checkpoint	PMID:21873635^[25]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1100512 PANTHER:PTN000015646 PomBase:SPAC13C5.07	P	Seeded From UniProt	complete
enables	GO:0008408	3'-5' exonuclease activity	PMID:21873635^[25]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002228124 SGD:S000004837 UniProtKB:P49959	F	Seeded From UniProt	complete
enables	GO:0008296	3'-5'-exodeoxyribonuclease activity	PMID:21873635^[25]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002228124 SGD:S000004837	F	Seeded From UniProt	complete
involved_in	GO:0007095	mitotic G2 DNA damage checkpoint	PMID:21873635^[25]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0020270 MGI:MGI:1100512 PANTHER:PTN000015644	P	Seeded From UniProt	complete
involved_in	GO:0006303	double-strand break repair via nonhomologous end joining	PMID:21873635^[25]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000015644 PomBase:SPAC13C5.07 SGD:S000004837 UniProtKB:P49959	P	Seeded From UniProt	complete
colocalizes_with	GO:0000784	nuclear chromosome, telomeric region	PMID:21873635^[25]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1100512 PANTHER:PTN000015644 PomBase:SPAC13C5.07 UniProtKB:P49959	C	Seeded From UniProt	complete
involved_in	GO:0000724	double-strand break repair via homologous recombination	PMID:21873635^[25]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000015644 PomBase:SPAC13C5.07 SGD:S000004837 UniProtKB:P49959	P	Seeded From UniProt	complete
involved_in	GO:0000723	telomere maintenance	PMID:21873635^[25]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0020270 PANTHER:PTN000015644 PomBase:SPAC13C5.07 SGD:S000004837 UniProtKB:P49959	P	Seeded From UniProt	complete
enables	GO:0008296	3'-5'-exodeoxyribonuclease activity	PMID:9858579^[1]	ECO:0000269	experimental evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008296	3'-5'-exodeoxyribonuclease activity	PMID:9845372^[16]	ECO:0000269	experimental evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008296	3'-5'-exodeoxyribonuclease activity	PMID:9799249^[26]	ECO:0000269	experimental evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008296	3'-5'-exodeoxyribonuclease activity	PMID:11454871^[17]	ECO:0000269	experimental evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0046940	nucleoside monophosphate phosphorylation	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004017	P	Seeded From UniProt	complete
enables	GO:0004519	endonuclease activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003701 InterPro:IPR007281	F	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR007281	C	Seeded From UniProt	complete
involved_in	GO:0006302	double-strand break repair	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003701 InterPro:IPR007281	P	Seeded From UniProt	complete
enables	GO:0008408	3'-5' exonuclease activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003701	F	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004843	F	Seeded From UniProt	complete
enables	GO:0030145	manganese ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR007281	F	Seeded From UniProt	complete
part_of	GO:0030870	Mre11 complex	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003701	C	Seeded From UniProt	complete
involved_in	GO:0042138	meiotic DNA double-strand break formation	PMID:9334324^[27]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0000706	meiotic DNA double-strand break processing	PMID:9334324^[27]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-SCE-981784	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt	complete
enables	GO:0004519	endonuclease activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0255	F	Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0234	P	Seeded From UniProt	complete
involved_in	GO:0051321	meiotic cell cycle	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0469	P	Seeded From UniProt	complete
enables	GO:0004518	nuclease activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0540	F	Seeded From UniProt	complete
enables	GO:0004527	exonuclease activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0269	F	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C	Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0227	P	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 Moreau, S et al. (1999) The nuclease activity of Mre11 is required for meiosis but not for mating type switching, end joining, or telomere maintenance. Mol. Cell. Biol. 19 556-66 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Ogawa, H et al. (1995) Functions of the yeast meiotic recombination genes, MRE11 and MRE2. Adv. Biophys. 31 67-76 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 Garcia, V et al. (2011) Bidirectional resection of DNA double-strand breaks by Mre11 and Exo1. Nature 479 241-4 PubMed GONUTS page
↑ Oh, J et al. (2016) Xrs2 Dependent and Independent Functions of the Mre11-Rad50 Complex. Mol. Cell 64 405-415 PubMed GONUTS page
↑ Reinders, J et al. (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J. Proteome Res. 5 1543-54 PubMed GONUTS page
↑ Tkach, JM et al. (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat. Cell Biol. 14 966-76 PubMed GONUTS page
↑ Sickmann, A et al. (2003) The proteome of Saccharomyces cerevisiae mitochondria. Proc. Natl. Acad. Sci. U.S.A. 100 13207-12 PubMed GONUTS page
↑ Ye, Y et al. (2016) The Saccharomyces cerevisiae Mre11-Rad50-Xrs2 complex promotes trinucleotide repeat expansions independently of homologous recombination. DNA Repair (Amst.) 43 1-8 PubMed GONUTS page
↑ ^9.0 ^9.1 Boulton, SJ & Jackson, SP (1998) Components of the Ku-dependent non-homologous end-joining pathway are involved in telomeric length maintenance and telomeric silencing. EMBO J. 17 1819-28 PubMed GONUTS page
↑ Muñoz-Galván, S et al. (2013) Competing roles of DNA end resection and non-homologous end joining functions in the repair of replication-born double-strand breaks by sister-chromatid recombination. Nucleic Acids Res. 41 1669-83 PubMed GONUTS page
↑ Kalifa, L et al. (2012) Mitochondrial genome maintenance: roles for nuclear nonhomologous end-joining proteins in Saccharomyces cerevisiae. Genetics 190 951-64 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 Ghosal, G & Muniyappa, K (2007) The characterization of Saccharomyces cerevisiae Mre11/Rad50/Xrs2 complex reveals that Rad50 negatively regulates Mre11 endonucleolytic but not the exonucleolytic activity. J. Mol. Biol. 372 864-82 PubMed GONUTS page
↑ ^13.0 ^13.1 Kugou, K et al. (2007) Mre11 mediates gene regulation in yeast spore development. Genes Genet. Syst. 82 21-33 PubMed GONUTS page
↑ ^14.0 ^14.1 Ghosal, G & Muniyappa, K (2005) Saccharomyces cerevisiae Mre11 is a high-affinity G4 DNA-binding protein and a G-rich DNA-specific endonuclease: implications for replication of telomeric DNA. Nucleic Acids Res. 33 4692-703 PubMed GONUTS page
↑ Takata, H et al. (2005) Late S phase-specific recruitment of Mre11 complex triggers hierarchical assembly of telomere replication proteins in Saccharomyces cerevisiae. Mol. Cell 17 573-83 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 ^16.3 ^16.4 Usui, T et al. (1998) Complex formation and functional versatility of Mre11 of budding yeast in recombination. Cell 95 705-16 PubMed GONUTS page
↑ ^17.0 ^17.1 Trujillo, KM & Sung, P (2001) DNA structure-specific nuclease activities in the Saccharomyces cerevisiae Rad50*Mre11 complex. J. Biol. Chem. 276 35458-64 PubMed GONUTS page
↑ Ajimura, M et al. (1993) Identification of new genes required for meiotic recombination in Saccharomyces cerevisiae. Genetics 133 51-66 PubMed GONUTS page
↑ Wilson, TE (2002) A genomics-based screen for yeast mutants with an altered recombination/end-joining repair ratio. Genetics 162 677-88 PubMed GONUTS page
↑ Steininger, S et al. (2010) A novel function for the Mre11-Rad50-Xrs2 complex in base excision repair. Nucleic Acids Res. 38 1853-65 PubMed GONUTS page
↑ Johzuka, K & Ogawa, H (1995) Interaction of Mre11 and Rad50: two proteins required for DNA repair and meiosis-specific double-strand break formation in Saccharomyces cerevisiae. Genetics 139 1521-32 PubMed GONUTS page
↑ Tsukamoto, Y et al. (2005) Xrs2p regulates Mre11p translocation to the nucleus and plays a role in telomere elongation and meiotic recombination. Mol. Biol. Cell 16 597-608 PubMed GONUTS page
↑ Bhaskara, V et al. (2007) Rad50 adenylate kinase activity regulates DNA tethering by Mre11/Rad50 complexes. Mol. Cell 25 647-61 PubMed GONUTS page
↑ ^24.0 ^24.1 Krishna, S et al. (2007) Mre11 and Ku regulation of double-strand break repair by gene conversion and break-induced replication. DNA Repair (Amst.) 6 797-808 PubMed GONUTS page
↑ ^25.0 ^25.1 ^25.2 ^25.3 ^25.4 ^25.5 ^25.6 ^25.7 ^25.8 ^25.9 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Furuse, M et al. (1998) Distinct roles of two separable in vitro activities of yeast Mre11 in mitotic and meiotic recombination. EMBO J. 17 6412-25 PubMed GONUTS page
↑ ^27.0 ^27.1 Roeder, GS (1997) Meiotic chromosomes: it takes two to tango. Genes Dev. 11 2600-21 PubMed GONUTS page

[PMID:9858579-1] 1.0 ^1.1 ^1.2 Moreau, S et al. (1999) The nuclease activity of Mre11 is required for meiosis but not for mating type switching, end joining, or telomere maintenance. Mol. Cell. Biol. 19 556-66 PubMed GONUTS page

[PMID:7625279-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Ogawa, H et al. (1995) Functions of the yeast meiotic recombination genes, MRE11 and MRE2. Adv. Biophys. 31 67-76 PubMed GONUTS page

[PMID:22002605-3] 3.0 ^3.1 ^3.2 ^3.3 Garcia, V et al. (2011) Bidirectional resection of DNA double-strand breaks by Mre11 and Exo1. Nature 479 241-4 PubMed GONUTS page

[PMID:27746018-4] Oh, J et al. (2016) Xrs2 Dependent and Independent Functions of the Mre11-Rad50 Complex. Mol. Cell 64 405-415 PubMed GONUTS page

[PMID:16823961-5] Reinders, J et al. (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J. Proteome Res. 5 1543-54 PubMed GONUTS page

[PMID:22842922-6] Tkach, JM et al. (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat. Cell Biol. 14 966-76 PubMed GONUTS page

[PMID:14576278-7] Sickmann, A et al. (2003) The proteome of Saccharomyces cerevisiae mitochondria. Proc. Natl. Acad. Sci. U.S.A. 100 13207-12 PubMed GONUTS page

[PMID:27173583-8] Ye, Y et al. (2016) The Saccharomyces cerevisiae Mre11-Rad50-Xrs2 complex promotes trinucleotide repeat expansions independently of homologous recombination. DNA Repair (Amst.) 43 1-8 PubMed GONUTS page

[PMID:9501103-9] 9.0 ^9.1 Boulton, SJ & Jackson, SP (1998) Components of the Ku-dependent non-homologous end-joining pathway are involved in telomeric length maintenance and telomeric silencing. EMBO J. 17 1819-28 PubMed GONUTS page

[PMID:23254329-10] Muñoz-Galván, S et al. (2013) Competing roles of DNA end resection and non-homologous end joining functions in the repair of replication-born double-strand breaks by sister-chromatid recombination. Nucleic Acids Res. 41 1669-83 PubMed GONUTS page

[PMID:22214610-11] Kalifa, L et al. (2012) Mitochondrial genome maintenance: roles for nuclear nonhomologous end-joining proteins in Saccharomyces cerevisiae. Genetics 190 951-64 PubMed GONUTS page

[PMID:17698079-12] 12.0 ^12.1 ^12.2 Ghosal, G & Muniyappa, K (2007) The characterization of Saccharomyces cerevisiae Mre11/Rad50/Xrs2 complex reveals that Rad50 negatively regulates Mre11 endonucleolytic but not the exonucleolytic activity. J. Mol. Biol. 372 864-82 PubMed GONUTS page

[PMID:17396017-13] 13.0 ^13.1 Kugou, K et al. (2007) Mre11 mediates gene regulation in yeast spore development. Genes Genet. Syst. 82 21-33 PubMed GONUTS page

[PMID:16116037-14] 14.0 ^14.1 Ghosal, G & Muniyappa, K (2005) Saccharomyces cerevisiae Mre11 is a high-affinity G4 DNA-binding protein and a G-rich DNA-specific endonuclease: implications for replication of telomeric DNA. Nucleic Acids Res. 33 4692-703 PubMed GONUTS page

[PMID:15721260-15] Takata, H et al. (2005) Late S phase-specific recruitment of Mre11 complex triggers hierarchical assembly of telomere replication proteins in Saccharomyces cerevisiae. Mol. Cell 17 573-83 PubMed GONUTS page

[PMID:9845372-16] 16.0 ^16.1 ^16.2 ^16.3 ^16.4 Usui, T et al. (1998) Complex formation and functional versatility of Mre11 of budding yeast in recombination. Cell 95 705-16 PubMed GONUTS page

[PMID:11454871-17] 17.0 ^17.1 Trujillo, KM & Sung, P (2001) DNA structure-specific nuclease activities in the Saccharomyces cerevisiae Rad50*Mre11 complex. J. Biol. Chem. 276 35458-64 PubMed GONUTS page

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[PMID:12399380-19] Wilson, TE (2002) A genomics-based screen for yeast mutants with an altered recombination/end-joining repair ratio. Genetics 162 677-88 PubMed GONUTS page

[PMID:20040573-20] Steininger, S et al. (2010) A novel function for the Mre11-Rad50-Xrs2 complex in base excision repair. Nucleic Acids Res. 38 1853-65 PubMed GONUTS page

[PMID:7789757-21] Johzuka, K & Ogawa, H (1995) Interaction of Mre11 and Rad50: two proteins required for DNA repair and meiosis-specific double-strand break formation in Saccharomyces cerevisiae. Genetics 139 1521-32 PubMed GONUTS page

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YEAST:MRE11

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