SPO12_ARATH
ID SPO12_ARATH Reviewed; 383 AA.
AC Q9M4A1; Q9SH50;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Meiotic recombination protein SPO11-2;
DE Short=AtSPO11-2;
DE EC=5.6.2.2 {ECO:0000305};
GN Name=SPO11-2; OrderedLocusNames=At1g63990; ORFNames=F22C12.24;
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], AND TISSUE SPECIFICITY.
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [5]
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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
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 [7]
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, ACTIVE SITE, AND
RP MUTAGENESIS OF TYR-124.
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 [9]
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 [10]
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 [11]
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:17018031, PubMed:17965269,
CC PubMed:26917763). Together with MTOPVIB, mediates DNA cleavage that
CC forms the double-strand breaks (DSB) that initiate meiotic
CC recombination (PubMed:26917763, PubMed:19763177). The complex promotes
CC relaxation of negative and positive supercoiled DNA and DNA
CC decatenation through cleavage and ligation cycles (PubMed:17018031,
CC PubMed:17965269, PubMed:26917763). {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 SPO11-1. 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 Q9M4A1; Q5Q0E6: MTOPVIB; NbExp=7; IntAct=EBI-1772309, EBI-16200362;
CC Q9M4A1; Q9M4A2: SPO11-1; NbExp=7; IntAct=EBI-1772309, EBI-1540725;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17018031,
CC ECO:0000269|PubMed:17965269}.
CC -!- TISSUE SPECIFICITY: Very low expression in flowers and shoots.
CC {ECO:0000269|PubMed:10710421}.
CC -!- DISRUPTION PHENOTYPE: Plants show a semi-sterile phenotype and a
CC drastic decrease of meiotic recombination, indicating that SPO11-1 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:17018031,
CC ECO:0000269|PubMed:17965269, ECO:0000269|PubMed:19763177}.
CC -!- SIMILARITY: Belongs to the TOP6A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF24569.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ251990; CAB81545.1; -; mRNA.
DR EMBL; AC007764; AAF24569.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34178.1; -; Genomic_DNA.
DR EMBL; DQ446392; ABE65738.1; -; mRNA.
DR PIR; A96665; A96665.
DR PIR; T52651; T52651.
DR RefSeq; NP_176582.2; NM_105072.3.
DR AlphaFoldDB; Q9M4A1; -.
DR SMR; Q9M4A1; -.
DR DIP; DIP-40433N; -.
DR IntAct; Q9M4A1; 3.
DR STRING; 3702.AT1G63990.1; -.
DR PaxDb; Q9M4A1; -.
DR PRIDE; Q9M4A1; -.
DR EnsemblPlants; AT1G63990.1; AT1G63990.1; AT1G63990.
DR GeneID; 842702; -.
DR Gramene; AT1G63990.1; AT1G63990.1; AT1G63990.
DR KEGG; ath:AT1G63990; -.
DR Araport; AT1G63990; -.
DR TAIR; locus:2024598; AT1G63990.
DR eggNOG; KOG2795; Eukaryota.
DR HOGENOM; CLU_037229_1_2_1; -.
DR InParanoid; Q9M4A1; -.
DR OMA; CTRSLMR; -.
DR OrthoDB; 1272299at2759; -.
DR PhylomeDB; Q9M4A1; -.
DR PRO; PR:Q9M4A1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9M4A1; baseline and differential.
DR Genevisible; Q9M4A1; AT.
DR GO; GO:0000228; C:nuclear chromosome; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
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:0007059; P:chromosome segregation; IMP:TAIR.
DR GO; GO:0009553; P:embryo sac development; IMP:TAIR.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:TAIR.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:TAIR.
DR GO; GO:0042138; P:meiotic DNA double-strand break formation; IBA:GO_Central.
DR GO; GO:0000706; P:meiotic DNA double-strand break processing; IBA:GO_Central.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:TAIR.
DR GO; GO:0048316; P:seed development; IMP:TAIR.
DR CDD; cd00223; TOPRIM_TopoIIB_SPO; 1.
DR Gene3D; 1.10.10.10; -; 1.
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; PR01550; TOP6AFAMILY.
DR SUPFAM; SSF56726; SSF56726; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Hydrolase; Isomerase; Magnesium; Meiosis; Metal-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..383
FT /note="Meiotic recombination protein SPO11-2"
FT /id="PRO_0000346111"
FT ACT_SITE 124
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:17965269"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q57815"
FT BINDING 270
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q57815"
FT MUTAGEN 124
FT /note="Y->F: Loss of double-strand breaks induction."
FT /evidence="ECO:0000269|PubMed:17965269"
SQ SEQUENCE 383 AA; 43126 MW; 08AB5FA102A1F189 CRC64;
MEESSGLSSM KFFSDQHLSY ADILLPHEAR ARIEVSVLNL LRILNSPDPA ISDLSLINRK
RSNSCINKGI LTDVSYIFLS TSFTKSSLTN AKTAKAFVRV WKVMEICFQI LLQEKRVTQR
ELFYKLLCDS PDYFSSQIEV NRSVQDVVAL LRCSRYSLGI MASSRGLVAG RLFLQEPGKE
AVDCSACGSS GFAITGDLNL LDNTIMRTDA RYIIIVEKHA IFHRLVEDRV FNHIPCVFIT
AKGYPDIATR FFLHRMSTTF PDLPILVLVD WNPAGLAILC TFKFGSIGMG LEAYRYACNV
KWIGLRGDDL NLIPEESLVP LKPKDSQIAK SLLSSKILQE NYIEELSLMV QTGKRAEIEA
LYCHGYNYLG KYIATKIVQG KYI
