SPO11_ARATH
ID SPO11_ARATH Reviewed; 362 AA.
AC Q9M4A2; Q9C5S3; Q9LK56;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Meiotic recombination protein SPO11-1 {ECO:0000303|PubMed:10710421};
DE Short=AtSPO11-1 {ECO:0000303|PubMed:10710421};
DE EC=5.6.2.2 {ECO:0000305};
GN Name=SPO11-1 {ECO:0000303|PubMed:10710421};
GN OrderedLocusNames=At3g13170 {ECO:0000312|Araport:AT3G13170};
GN ORFNames=MJG19.19 {ECO:0000312|EMBL:AAK21002.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
RC STRAIN=cv. Columbia; TISSUE=Flower;
RX PubMed=10710421; DOI=10.1093/nar/28.7.1548;
RA Hartung F., Puchta H.;
RT "Molecular characterisation of two paralogous SPO11 homologues in
RT Arabidopsis thaliana.";
RL Nucleic Acids Res. 28:1548-1554(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP ALTERNATIVE SPLICING.
RC STRAIN=cv. Wassilewskija;
RX PubMed=11157765; DOI=10.1093/emboj/20.3.589;
RA Grelon M., Vezon D., Gendrot G., Pelletier G.;
RT "AtSPO11-1 is necessary for efficient meiotic recombination in plants.";
RL EMBO J. 20:589-600(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP LACK OF INTERACTION WITH TOP6B.
RC STRAIN=cv. Columbia; TISSUE=Flower;
RX PubMed=11410368; DOI=10.1016/s0378-1119(01)00496-6;
RA Hartung F., Puchta H.;
RT "Molecular characterization of homologues of both subunits A (SPO11) and B
RT of the archaebacterial topoisomerase 6 in plants.";
RL Gene 271:81-86(2001).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17018031; DOI=10.1111/j.1365-313x.2006.02867.x;
RA Stacey N.J., Kuromori T., Azumi Y., Roberts G., Breuer C., Wada T.,
RA Maxwell A., Roberts K., Sugimoto-Shirasu K.;
RT "Arabidopsis SPO11-2 functions with SPO11-1 in meiotic recombination.";
RL Plant J. 48:206-216(2006).
RN [8]
RP INTERACTION WITH PRD1.
RX PubMed=17762870; DOI=10.1038/sj.emboj.7601815;
RA De Muyt A., Vezon D., Gendrot G., Gallois J.-L., Stevens R., Grelon M.;
RT "AtPRD1 is required for meiotic double strand break formation in
RT Arabidopsis thaliana.";
RL EMBO J. 26:4126-4137(2007).
RN [9]
RP FUNCTION, ACTIVE SITE, AND MUTAGENESIS OF TYR-103.
RX PubMed=17965269; DOI=10.1105/tpc.107.054817;
RA Hartung F., Wurz-Wildersinn R., Fuchs J., Schubert I., Suer S., Puchta H.;
RT "The catalytically active tyrosine residues of both SPO11-1 and SPO11-2 are
RT required for meiotic double-strand break induction in Arabidopsis.";
RL Plant Cell 19:3090-3099(2007).
RN [10]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=17785529; DOI=10.1101/gad.439007;
RA Sanchez-Moran E., Santos J.-L., Jones G.H., Franklin F.C.;
RT "ASY1 mediates AtDMC1-dependent interhomolog recombination during meiosis
RT in Arabidopsis.";
RL Genes Dev. 21:2220-2233(2007).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19763177; DOI=10.1371/journal.pgen.1000654;
RA De Muyt A., Pereira L., Vezon D., Chelysheva L., Gendrot G., Chambon A.,
RA Laine-Choinard S., Pelletier G., Mercier R., Nogue F., Grelon M.;
RT "A high throughput genetic screen identifies new early meiotic
RT recombination functions in Arabidopsis thaliana.";
RL PLoS Genet. 5:E1000654-E1000654(2009).
RN [12]
RP FUNCTION, AND INTERACTION WITH MTOPVIB.
RX PubMed=26917763; DOI=10.1126/science.aad5196;
RA Vrielynck N., Chambon A., Vezon D., Pereira L., Chelysheva L., De Muyt A.,
RA Mezard C., Mayer C., Grelon M.;
RT "A DNA topoisomerase VI-like complex initiates meiotic recombination.";
RL Science 351:939-943(2016).
RN [13]
RP INTERACTION WITH MTOPVIB AND PRD1.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=28855712; DOI=10.1038/s41598-017-10270-9;
RA Tang Y., Yin Z., Zeng Y., Zhang Q., Chen L., He Y., Lu P., Ye D., Zhang X.;
RT "MTOPVIB interacts with AtPRD1 and plays important roles in formation of
RT meiotic DNA double-strand breaks in Arabidopsis.";
RL Sci. Rep. 7:10007-10007(2017).
CC -!- FUNCTION: Component of a topoisomerase 6 complex specifically required
CC for meiotic recombination (PubMed:11157765, PubMed:17018031,
CC PubMed:17965269, PubMed:26917763). Together with MTOPVIB, mediates DNA
CC cleavage that forms the double-strand breaks (DSB) that initiate
CC meiotic recombination (PubMed:26917763, PubMed:19763177). The complex
CC promotes relaxation of negative and positive supercoiled DNA and DNA
CC decatenation through cleavage and ligation cycles (PubMed:11157765,
CC PubMed:17018031, PubMed:17965269, PubMed:26917763).
CC {ECO:0000269|PubMed:11157765, ECO:0000269|PubMed:17018031,
CC ECO:0000269|PubMed:17965269, ECO:0000269|PubMed:19763177,
CC ECO:0000269|PubMed:26917763}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q57815};
CC -!- SUBUNIT: Heterotetramer of 2 SPO11 (SPO11-1 and/or SPO11-2) and 2
CC MTOPVIB chains (Probable). Interacts with MTOPVIB (PubMed:26917763,
CC PubMed:28855712). May form a heterodimer with SPO11-2. Interacts with
CC PRD1 (PubMed:17762870, PubMed:28855712). Does not interact with TOP6B
CC (PubMed:11410368). {ECO:0000269|PubMed:11410368,
CC ECO:0000269|PubMed:17762870, ECO:0000269|PubMed:26917763,
CC ECO:0000269|PubMed:28855712}.
CC -!- INTERACTION:
CC Q9M4A2; Q5Q0E6: MTOPVIB; NbExp=6; IntAct=EBI-1540725, EBI-16200362;
CC Q9M4A2; Q9M4A1: SPO11-2; NbExp=7; IntAct=EBI-1540725, EBI-1772309;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17785529}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9M4A2-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in shoots, young seedlings, flowers and
CC reproductive tissues. Not found in roots or rosette leaves.
CC {ECO:0000269|PubMed:10710421}.
CC -!- DEVELOPMENTAL STAGE: Accumulates in early G2 phase and then disappears
CC over a period of between 1 and 5 hours post-S phase.
CC {ECO:0000269|PubMed:17785529}.
CC -!- DISRUPTION PHENOTYPE: Plants show a semi-sterile phenotype and a
CC drastic decrease of meiotic recombination, indicating that SPO11-2 and
CC SPO11-3 are not functionally redundant. SPO11-1 and SPO11-2 are both
CC required for double-strand breaks induction. Drastic decrease in
CC chiasma formation at metaphase I associated with an absence of synapsis
CC in prophase, due to the inability to make double-strand breaks (DSB)
CC (PubMed:19763177). {ECO:0000269|PubMed:11157765,
CC ECO:0000269|PubMed:17018031, ECO:0000269|PubMed:19763177}.
CC -!- SIMILARITY: Belongs to the TOP6A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01408.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ251989; CAB81544.1; -; mRNA.
DR EMBL; AF302928; AAK21002.1; -; Genomic_DNA.
DR EMBL; AP000375; BAB01408.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75304.1; -; Genomic_DNA.
DR EMBL; BT028955; ABI49502.1; -; mRNA.
DR PIR; T52652; T52652.
DR RefSeq; NP_187923.1; NM_112156.2. [Q9M4A2-1]
DR AlphaFoldDB; Q9M4A2; -.
DR SMR; Q9M4A2; -.
DR DIP; DIP-62004N; -.
DR IntAct; Q9M4A2; 3.
DR MINT; Q9M4A2; -.
DR STRING; 3702.AT3G13170.1; -.
DR PaxDb; Q9M4A2; -.
DR PRIDE; Q9M4A2; -.
DR EnsemblPlants; AT3G13170.1; AT3G13170.1; AT3G13170. [Q9M4A2-1]
DR GeneID; 820506; -.
DR Gramene; AT3G13170.1; AT3G13170.1; AT3G13170. [Q9M4A2-1]
DR KEGG; ath:AT3G13170; -.
DR Araport; AT3G13170; -.
DR TAIR; locus:2090044; AT3G13170.
DR eggNOG; KOG2795; Eukaryota.
DR HOGENOM; CLU_037229_1_1_1; -.
DR OMA; TKRNIYY; -.
DR PhylomeDB; Q9M4A2; -.
DR PRO; PR:Q9M4A2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M4A2; baseline and differential.
DR Genevisible; Q9M4A2; AT.
DR GO; GO:0000228; C:nuclear chromosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051026; P:chiasma assembly; IMP:TAIR.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:EnsemblPlants.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:TAIR.
DR GO; GO:0042138; P:meiotic DNA double-strand break formation; IGI:TAIR.
DR GO; GO:0000706; P:meiotic DNA double-strand break processing; IBA:GO_Central.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:TAIR.
DR CDD; cd00223; TOPRIM_TopoIIB_SPO; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR013048; Meiotic_Spo11.
DR InterPro; IPR002815; Spo11/TopoVI_A.
DR InterPro; IPR013049; Spo11/TopoVI_A_N.
DR InterPro; IPR036078; Spo11/TopoVI_A_sf.
DR InterPro; IPR034136; TOPRIM_Topo6A/Spo11.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR10848; PTHR10848; 1.
DR Pfam; PF04406; TP6A_N; 1.
DR PRINTS; PR01551; SPO11HOMOLOG.
DR PRINTS; PR01550; TOP6AFAMILY.
DR SUPFAM; SSF56726; SSF56726; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Hydrolase; Isomerase; Magnesium;
KW Meiosis; Metal-binding; Nucleus; Reference proteome.
FT CHAIN 1..362
FT /note="Meiotic recombination protein SPO11-1"
FT /id="PRO_0000346110"
FT ACT_SITE 103
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:17965269"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q57815"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q57815"
FT MUTAGEN 103
FT /note="Y->F: Loss of double-strand breaks induction."
FT /evidence="ECO:0000269|PubMed:17965269"
FT CONFLICT 5
FT /note="F -> I (in Ref. 2; AAK21002)"
FT /evidence="ECO:0000305"
FT CONFLICT 10
FT /note="S -> T (in Ref. 2; AAK21002)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="V -> E (in Ref. 2; AAK21002)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="N -> S (in Ref. 2; AAK21002)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="F -> L (in Ref. 2; AAK21002)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="V -> I (in Ref. 2; AAK21002)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="V -> L (in Ref. 2; AAK21002)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 41804 MW; AE82942C4F456770 CRC64;
MEGKFAISES TNLLQRIKDF TQSVVVDLAE GRSPKISINQ FRNYCMNPEA DCLCSSDKPK
GQEIFTLKKE PQTYRIDMLL RVLLIVQQLL QENRHASKRD IYYMHPSAFK AQSIVDRAIG
DICILFQCSR YNLNVVSVGN GLVMGWLKFR EAGRKFDCLN SLNTAYPVPV LVEEVEDIVS
LAEYILVVEK ETVFQRLAND MFCKTNRCIV ITGRGYPDVS TRRFLRLLME KLHLPVHCLV
DCDPYGFEIL ATYRFGSMQM AYDIESLRAP DMKWLGAFPS DSEVYSVPKQ CLLPLTEEDK
KRTEAMLLRC YLKREMPQWR LELETMLKRG VKFEIEALSV HSLSFLSEVY IPSKIRREVS
SP
