XRN1_YEAST
ID XRN1_YEAST Reviewed; 1528 AA.
AC P22147; D6VTX9;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=5'-3' exoribonuclease 1;
DE EC=3.1.13.-;
DE AltName: Full=DNA strand transfer protein beta;
DE Short=STP-beta;
DE AltName: Full=KAR(-)-enhancing mutation protein;
DE AltName: Full=Strand exchange protein 1;
DE AltName: Full=p175;
GN Name=XRN1; Synonyms=DST2, KEM1, RAR5, SEP1, SKI1;
GN OrderedLocusNames=YGL173C; ORFNames=G1645;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=2076815; DOI=10.1093/genetics/126.4.799;
RA Kim J., Ljungdahl P.O., Fink G.R.;
RT "kem mutations affect nuclear fusion in Saccharomyces cerevisiae.";
RL Genetics 126:799-812(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1840632; DOI=10.1128/mcb.11.5.2593-2608.1991;
RA Tishkoff D., Johnson A.W., Kolodner R.D.;
RT "Molecular and genetic analysis of the gene encoding the Saccharomyces
RT cerevisiae strand exchange protein Sep1.";
RL Mol. Cell. Biol. 11:2593-2608(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204626 / S288c / A364A;
RX PubMed=1850100; DOI=10.1128/mcb.11.5.2583-2592.1991;
RA Dykstra C.C., Kitada K., Clark A.B., Hamatake R.K., Sugino A.;
RT "Cloning and characterization of DST2, the gene for DNA strand transfer
RT protein beta from Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 11:2583-2592(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1979303; DOI=10.1016/0378-1119(90)90417-p;
RA Larimer F.W., Stevens A.;
RT "Disruption of the gene XRN1, coding for a 5'-->3' exoribonuclease,
RT restricts yeast cell growth.";
RL Gene 95:85-90(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RX PubMed=2027746; DOI=10.1093/nar/19.7.1385;
RA Kipling D., Tambini C., Kearsey S.E.;
RT "rar mutations which increase artificial chromosome stability in
RT Saccharomyces cerevisiae identify transcription and recombination
RT proteins.";
RL Nucleic Acids Res. 19:1385-1391(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8619317; DOI=10.1002/yea.320111209;
RA Bertani I., Coglievina M., Zaccaria P., Klima R., Bruschi C.V.;
RT "The sequence of an 11.1 kb fragment on the left arm of Saccharomyces
RT cerevisiae chromosome VII reveals six open reading frames including NSP49,
RT KEM1 and four putative new genes.";
RL Yeast 11:1187-1194(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [8]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [9]
RP CHARACTERIZATION OF EXONUCLEASE ACTIVITY.
RX PubMed=1856231; DOI=10.1016/s0021-9258(18)92808-5;
RA Johnson A.W., Kolodner R.D.;
RT "Strand exchange protein 1 from Saccharomyces cerevisiae. A novel
RT multifunctional protein that contains DNA strand exchange and exonuclease
RT activities.";
RL J. Biol. Chem. 266:14046-14054(1991).
RN [10]
RP CHARACTERIZATION OF EXORIBONUCLEASE ACTIVITY.
RX PubMed=1398123; DOI=10.1016/0378-1119(92)90008-d;
RA Larimer F.W., Hsu C.L., Maupin M.K., Stevens A.;
RT "Characterization of the XRN1 gene encoding a 5'-->3' exoribonuclease:
RT sequence data and analysis of disparate protein and mRNA levels of gene-
RT disrupted yeast cells.";
RL Gene 120:51-57(1992).
RN [11]
RP FUNCTION.
RX PubMed=7926736; DOI=10.1101/gad.8.11.1356;
RA Chen J., Kanaar R., Cozzarelli N.R.;
RT "The Sep1 strand exchange protein from Saccharomyces cerevisiae promotes a
RT paranemic joint between homologous DNA molecules.";
RL Genes Dev. 8:1356-1366(1994).
RN [12]
RP CHARACTERIZATION OF EXONUCLEASE ACTIVITY DURING STRAND EXCHANGE.
RX PubMed=8106411; DOI=10.1016/s0021-9258(17)41912-0;
RA Johnson A.W., Kolodner R.D.;
RT "The activity of the Saccharomyces cerevisiae strand exchange protein 1
RT intrinsic exonuclease during joint molecule formation.";
RL J. Biol. Chem. 269:3664-3672(1994).
RN [13]
RP DNA-BINDING PROPERTIES.
RX PubMed=8106412; DOI=10.1016/s0021-9258(17)41913-2;
RA Johnson A.W., Kolodner R.D.;
RT "Characterization of the interaction of Saccharomyces cerevisiae strand
RT exchange protein 1 with DNA.";
RL J. Biol. Chem. 269:3673-3681(1994).
RN [14]
RP CHARACTERIZATION OF EXONUCLEASE AND STRAND EXCHANGE ACTIVITIES.
RX PubMed=8188690; DOI=10.1016/s0021-9258(17)36759-5;
RA Kaeslin E., Heyer W.-D.;
RT "A multifunctional exonuclease from vegetative Schizosaccharomyces pombe
RT cells exhibiting in vitro strand exchange activity.";
RL J. Biol. Chem. 269:14094-14102(1994).
RN [15]
RP CHARACTERIZATION OF SPECIFICITY FOR G4 TETRAPLEX DNA.
RX PubMed=8020096; DOI=10.1016/0092-8674(94)90447-2;
RA Liu Z., Gilbert W.;
RT "The yeast KEM1 gene encodes a nuclease specific for G4 tetraplex DNA:
RT implication of in vivo functions for this novel DNA structure.";
RL Cell 77:1083-1092(1994).
RN [16]
RP ASSOCIATION WITH MICROTUBULES.
RX PubMed=7720696; DOI=10.1002/j.1460-2075.1995.tb07088.x;
RA Interthal H., Bellocq C., Baehler J., Bashkirov V.I., Edelstein S.J.,
RA Heyer W.-D.;
RT "A role of Sep1 (= Kem1, Xrn1) as a microtubule-associated protein in
RT Saccharomyces cerevisiae.";
RL EMBO J. 14:1057-1066(1995).
RN [17]
RP DISRUPTION PHENOTYPE.
RX PubMed=7713413; DOI=10.1093/genetics/139.2.495;
RA Tishkoff D.X., Rockmill B., Roeder G.S., Kolodner R.D.;
RT "The sep1 mutant of Saccharomyces cerevisiae arrests in pachytene and is
RT deficient in meiotic recombination.";
RL Genetics 139:495-509(1995).
RN [18]
RP SUBCELLULAR LOCATION.
RX PubMed=7739553; DOI=10.1128/mcb.15.5.2728;
RA Heyer W.-D., Johnson A.W., Reinhart U., Kolodner R.D.;
RT "Regulation and intracellular localization of Saccharomyces cerevisiae
RT strand exchange protein 1 (Sep1/Xrn1/Kem1), a multifunctional
RT exonuclease.";
RL Mol. Cell. Biol. 15:2728-2736(1995).
RN [19]
RP FUNCTION.
RX PubMed=7597069; DOI=10.1073/pnas.92.13.6002;
RA Liu Z., Lee A., Gilbert W.;
RT "Gene disruption of a G4-DNA-dependent nuclease in yeast leads to cellular
RT senescence and telomere shortening.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:6002-6006(1995).
RN [20]
RP FUNCTION.
RX PubMed=9315672; DOI=10.1128/mcb.17.10.6122;
RA Johnson A.W.;
RT "Rat1p and Xrn1p are functionally interchangeable exoribonucleases that are
RT restricted to and required in the nucleus and cytoplasm, respectively.";
RL Mol. Cell. Biol. 17:6122-6130(1997).
RN [21]
RP FUNCTION.
RX PubMed=9488433; DOI=10.1128/mcb.18.3.1181;
RA Petfalski E., Dandekar T., Henry Y., Tollervey D.;
RT "Processing of the precursors to small nucleolar RNAs and rRNAs requires
RT common components.";
RL Mol. Cell. Biol. 18:1181-1189(1998).
RN [22]
RP FUNCTION.
RX PubMed=9742129; DOI=10.1128/mcb.18.10.6121;
RA Lew J.E., Enomoto S., Berman J.;
RT "Telomere length regulation and telomeric chromatin require the nonsense-
RT mediated mRNA decay pathway.";
RL Mol. Cell. Biol. 18:6121-6130(1998).
RN [23]
RP FUNCTION, AND MUTAGENESIS OF ASN-37; HIS-41; ASP-86; GLY-87; LYS-93;
RP GLN-97; ARG-101; GLU-178; CYS-201; LEU-592; TYR-710; TRP-798; GLU-1024;
RP TYR-1043 AND SER-1197.
RX PubMed=9685486; DOI=10.1093/nar/26.16.3707;
RA Page A.M., Davis K., Molineux C., Kolodner R.D., Johnson A.W.;
RT "Mutational analysis of exoribonuclease I from Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 26:3707-3716(1998).
RN [24]
RP FUNCTION.
RX PubMed=9482746; DOI=10.1093/emboj/17.5.1497;
RA Anderson J.S.J., Parker R.P.;
RT "The 3' to 5' degradation of yeast mRNAs is a general mechanism for mRNA
RT turnover that requires the SKI2 DEVH box protein and 3' to 5' exonucleases
RT of the exosome complex.";
RL EMBO J. 17:1497-1506(1998).
RN [25]
RP FUNCTION, AND MUTAGENESIS OF ASP-206 AND ASP-208.
RX PubMed=10454540; DOI=10.1128/mcb.19.9.5930;
RA Solinger J.A., Pascolini D., Heyer W.-D.;
RT "Active-site mutations in the Xrn1p exoribonuclease of Saccharomyces
RT cerevisiae reveal a specific role in meiosis.";
RL Mol. Cell. Biol. 19:5930-5942(1999).
RN [26]
RP FUNCTION.
RX PubMed=11142370; DOI=10.1017/s1355838200001540;
RA Geerlings T.H., Vos J.C., Raue H.A.;
RT "The final step in the formation of 25S rRNA in Saccharomyces cerevisiae is
RT performed by 5'->3' exonucleases.";
RL RNA 6:1698-1703(2000).
RN [27]
RP FUNCTION.
RX PubMed=11238889; DOI=10.1128/mcb.21.5.1515-1530.2001;
RA He F., Jacobson A.;
RT "Upf1p, Nmd2p, and Upf3p regulate the decapping and exonucleolytic
RT degradation of both nonsense-containing mRNAs and wild-type mRNAs.";
RL Mol. Cell. Biol. 21:1515-1530(2001).
RN [28]
RP FUNCTION.
RX PubMed=12423748; DOI=10.1111/j.1574-6968.2002.tb11410.x;
RA Kim J., Kim J.;
RT "KEM1 is involved in filamentous growth of Saccharomyces cerevisiae.";
RL FEMS Microbiol. Lett. 216:33-38(2002).
RN [29]
RP FUNCTION.
RX PubMed=11910109; DOI=10.1126/science.1067338;
RA Frischmeyer P.A., van Hoof A., O'Donnell K., Guerrerio A.L., Parker R.,
RA Dietz H.C.;
RT "An mRNA surveillance mechanism that eliminates transcripts lacking
RT termination codons.";
RL Science 295:2258-2261(2002).
RN [30]
RP FUNCTION.
RX PubMed=14690598; DOI=10.1016/s1097-2765(03)00446-5;
RA He F., Li X., Spatrick P., Casillo R., Dong S., Jacobson A.;
RT "Genome-wide analysis of mRNAs regulated by the nonsense-mediated and 5' to
RT 3' mRNA decay pathways in yeast.";
RL Mol. Cell 12:1439-1452(2003).
RN [31]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [32]
RP FUNCTION.
RX PubMed=12799443; DOI=10.1093/nar/gkg430;
RA Kebaara B., Nazarenus T., Taylor R., Forch A., Atkin A.L.;
RT "The Upf-dependent decay of wild-type PPR1 mRNA depends on its 5'-UTR and
RT first 92 ORF nucleotides.";
RL Nucleic Acids Res. 31:3157-3165(2003).
RN [33]
RP FUNCTION.
RX PubMed=12853617; DOI=10.1093/nar/gkg474;
RA Heikkinen H.L., Llewellyn S.A., Barnes C.A.;
RT "Initiation-mediated mRNA decay in yeast affects heat-shock mRNAs, and
RT works through decapping and 5'-to-3' hydrolysis.";
RL Nucleic Acids Res. 31:4006-4016(2003).
RN [34]
RP FUNCTION.
RX PubMed=14561886; DOI=10.1261/rna.5126203;
RA Lee C.Y., Lee A., Chanfreau G.;
RT "The roles of endonucleolytic cleavage and exonucleolytic digestion in the
RT 5'-end processing of S. cerevisiae box C/D snoRNAs.";
RL RNA 9:1362-1370(2003).
RN [35]
RP SUBCELLULAR LOCATION.
RX PubMed=12730603; DOI=10.1126/science.1082320;
RA Sheth U., Parker R.;
RT "Decapping and decay of messenger RNA occur in cytoplasmic processing
RT bodies.";
RL Science 300:805-808(2003).
RN [36]
RP FUNCTION.
RX PubMed=15013450; DOI=10.1016/j.bbrc.2004.01.039;
RA Yano T., Inukai M., Isono F.;
RT "Deletion of OSH3 gene confers resistance against ISP-1 in Saccharomyces
RT cerevisiae.";
RL Biochem. Biophys. Res. Commun. 315:228-234(2004).
RN [37]
RP FUNCTION.
RX PubMed=15358132; DOI=10.1016/j.bbrc.2004.07.065;
RA Kim J., Jeon S., Yang Y.-S., Kim J.;
RT "Posttranscriptional regulation of the karyogamy gene by Kem1p/Xrn1p
RT exoribonuclease and Rok1p RNA helicase of Saccharomyces cerevisiae.";
RL Biochem. Biophys. Res. Commun. 321:1032-1039(2004).
RN [38]
RP FUNCTION.
RX PubMed=14729943; DOI=10.1128/mcb.24.3.945-953.2004;
RA Gill T., Cai T., Aulds J., Wierzbicki S., Schmitt M.E.;
RT "RNase MRP cleaves the CLB2 mRNA to promote cell cycle progression: novel
RT method of mRNA degradation.";
RL Mol. Cell. Biol. 24:945-953(2004).
RN [39]
RP FUNCTION.
RX PubMed=16240118; DOI=10.1007/s00294-005-0030-5;
RA Pathak R., Bogomolnaya L.M., Guo J., Polymenis M.;
RT "A role for KEM1 at the START of the cell cycle in Saccharomyces
RT cerevisiae.";
RL Curr. Genet. 48:300-309(2005).
RN [40]
RP FUNCTION.
RX PubMed=15967792; DOI=10.1074/jbc.m505913200;
RA Zer C., Chanfreau G.;
RT "Regulation and surveillance of normal and 3'-extended forms of the yeast
RT aci-reductone dioxygenase mRNA by RNase III cleavage and exonucleolytic
RT degradation.";
RL J. Biol. Chem. 280:28997-29003(2005).
RN [41]
RP FUNCTION.
RX PubMed=15989963; DOI=10.1016/j.molcel.2005.05.021;
RA Lee A., Henras A.K., Chanfreau G.;
RT "Multiple RNA surveillance pathways limit aberrant expression of iron
RT uptake mRNAs and prevent iron toxicity in S. cerevisiae.";
RL Mol. Cell 19:39-51(2005).
RN [42]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [43]
RP ACTIVITY REGULATION.
RX PubMed=16352596; DOI=10.1074/jbc.m511688200;
RA Todeschini A.-L., Condon C., Benard L.;
RT "Sodium-induced GCN4 expression controls the accumulation of the 5' to 3'
RT RNA degradation inhibitor, 3'-phosphoadenosine 5'-phosphate.";
RL J. Biol. Chem. 281:3276-3282(2006).
RN [44]
RP FUNCTION.
RX PubMed=16885161; DOI=10.1074/jbc.m601573200;
RA Jang L.-T., Buu L.-M., Lee F.-J.S.;
RT "Determinants of Rbp1p localization in specific cytoplasmic mRNA-processing
RT foci, P-bodies.";
RL J. Biol. Chem. 281:29379-29390(2006).
RN [45]
RP FUNCTION.
RX PubMed=16501073; DOI=10.1128/jvi.80.6.2631-2640.2006;
RA Cheng C.-P., Serviene E., Nagy P.D.;
RT "Suppression of viral RNA recombination by a host exoribonuclease.";
RL J. Virol. 80:2631-2640(2006).
RN [46]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16373495; DOI=10.1261/rna.2264806;
RA Beliakova-Bethell N., Beckham C., Giddings T.H. Jr., Winey M., Parker R.,
RA Sandmeyer S.;
RT "Virus-like particles of the Ty3 retrotransposon assemble in association
RT with P-body components.";
RL RNA 12:94-101(2006).
RN [47]
RP FUNCTION.
RX PubMed=16714281; DOI=10.1261/rna.46306;
RA Meaux S., Van Hoof A.;
RT "Yeast transcripts cleaved by an internal ribozyme provide new insight into
RT the role of the cap and poly(A) tail in translation and mRNA decay.";
RL RNA 12:1323-1337(2006).
RN [48]
RP DISRUPTION PHENOTYPE.
RX PubMed=17151231; DOI=10.1534/genetics.106.064428;
RA Lockshon D., Surface L.E., Kerr E.O., Kaeberlein M., Kennedy B.K.;
RT "The sensitivity of yeast mutants to oleic acid implicates the peroxisome
RT and other processes in membrane function.";
RL Genetics 175:77-91(2007).
RN [49]
RP FUNCTION.
RX PubMed=17761681; DOI=10.1074/jbc.m705098200;
RA Choi H.-S., Carman G.M.;
RT "Respiratory deficiency mediates the regulation of CHO1-encoded
RT phosphatidylserine synthase by mRNA stability in Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 282:31217-31227(2007).
RN [50]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [51]
RP SUBCELLULAR LOCATION.
RX PubMed=17429074; DOI=10.1091/mbc.e07-03-0199;
RA Teixeira D., Parker R.;
RT "Analysis of P-body assembly in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 18:2274-2287(2007).
RN [52]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1510, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [53]
RP FUNCTION.
RX PubMed=18443146; DOI=10.1101/gad.1654308;
RA Chernyakov I., Whipple J.M., Kotelawala L., Grayhack E.J., Phizicky E.M.;
RT "Degradation of several hypomodified mature tRNA species in Saccharomyces
RT cerevisiae is mediated by Met22 and the 5'-3' exonucleases Rat1 and Xrn1.";
RL Genes Dev. 22:1369-1380(2008).
RN [54]
RP FUNCTION.
RX PubMed=18676807; DOI=10.1101/gad.473608;
RA Goler-Baron V., Selitrennik M., Barkai O., Haimovich G., Lotan R.,
RA Choder M.;
RT "Transcription in the nucleus and mRNA decay in the cytoplasm are coupled
RT processes.";
RL Genes Dev. 22:2022-2027(2008).
RN [55]
RP SUBCELLULAR LOCATION.
RX PubMed=18689878; DOI=10.1534/genetics.108.091256;
RA Scarcelli J.J., Viggiano S., Hodge C.A., Heath C.V., Amberg D.C.,
RA Cole C.N.;
RT "Synthetic genetic array analysis in Saccharomyces cerevisiae provides
RT evidence for an interaction between RAT8/DBP5 and genes encoding P-body
RT components.";
RL Genetics 179:1945-1955(2008).
RN [56]
RP FUNCTION.
RX PubMed=18640978; DOI=10.1074/jbc.m804400200;
RA Esteban R., Vega L., Fujimura T.;
RT "20S RNA narnavirus defies the antiviral activity of SKI1/XRN1 in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 283:25812-25820(2008).
RN [57]
RP FUNCTION.
RX PubMed=18715869; DOI=10.1074/jbc.m804910200;
RA Pedro-Segura E., Vergara S.V., Rodriguez-Navarro S., Parker R.,
RA Thiele D.J., Puig S.;
RT "The Cth2 ARE-binding protein recruits the Dhh1 helicase to promote the
RT decay of succinate dehydrogenase SDH4 mRNA in response to iron
RT deficiency.";
RL J. Biol. Chem. 283:28527-28535(2008).
RN [58]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18162578; DOI=10.1091/mbc.e07-09-0954;
RA Beckham C., Hilliker A., Cziko A.-M., Noueiry A., Ramaswami M., Parker R.;
RT "The DEAD-box RNA helicase Ded1p affects and accumulates in Saccharomyces
RT cerevisiae P-bodies.";
RL Mol. Biol. Cell 19:984-993(2008).
RN [59]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1510, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [60]
RP FUNCTION.
RX PubMed=18469165; DOI=10.1261/rna.955508;
RA Rendl L.M., Bieman M.A., Smibert C.A.;
RT "S. cerevisiae Vts1p induces deadenylation-dependent transcript degradation
RT and interacts with the Ccr4p-Pop2p-Not deadenylase complex.";
RL RNA 14:1328-1336(2008).
RN [61]
RP FUNCTION.
RX PubMed=19324962; DOI=10.1261/rna.1458909;
RA Holbein S., Wengi A., Decourty L., Freimoser F.M., Jacquier A., Dichtl B.;
RT "Cordycepin interferes with 3' end formation in yeast independently of its
RT potential to terminate RNA chain elongation.";
RL RNA 15:837-849(2009).
RN [62]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1506 AND SER-1510, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Multifunctional protein that exhibits several independent
CC functions at different levels of the cellular processes. 5'-3'
CC exonuclease component of the nonsense-mediated mRNA decay (NMD) which
CC is a highly conserved mRNA degradation pathway, an RNA surveillance
CC system whose role is to identify and rid cells of mRNA with premature
CC termination codons and thus prevents accumulation of potentially
CC harmful truncated proteins. The NMD pathway has a second role
CC regulating the decay of wild-type mRNAs, and especially mRNAs that are
CC important for telomere functions. Participate in CTH2-mediated and
CC VTS1-mediated mRNA turnover. Involved in the degradation of several
CC hypomodified mature tRNA species and participates in the 5'-processing
CC or the degradation of the snoRNA precursors and rRNA processing.
CC Involved in defense against virus and suppresses viral RNA
CC recombination by rapidly removing the 5'-truncated RNAs, the substrates
CC of recombination, and thus reducing the chance for recombination to
CC occur in the parental strain. Required for the assembly of the virus-
CC like particles of the Ty3 retrotransposon and contributes to the
CC efficient generation of narnavirus 20S RNA by playing a major role in
CC the elimination of the non-viral upstream sequences from the primary
CC transcripts. Degrades single-stranded DNA (ss-DNA) and can renature
CC complementary ss-DNA as well as catalyzes the formation of heteroduplex
CC DNA from circular ss-DNA and homologous linear ds-DNA in vitro. Acts as
CC a microtubule-associated protein which interacts with cytoplasmic
CC microtubules through beta-tubulin and promotes in vitro assembly of
CC tubulin into microtubules. Associates with microtubule functions such
CC as chromosome transmission, nuclear migration, and SPB duplication. Has
CC also a role in G1 to S transition and is involved in nuclear fusion
CC during karyogamy. Required for the expression of ROK1 at the post-
CC transcriptional level and for the alpha-factor induction of the
CC karyogamy genes KAR3 and KAR4. Plays a role in filamentous growth.
CC {ECO:0000269|PubMed:10454540, ECO:0000269|PubMed:11142370,
CC ECO:0000269|PubMed:11238889, ECO:0000269|PubMed:11910109,
CC ECO:0000269|PubMed:12423748, ECO:0000269|PubMed:12799443,
CC ECO:0000269|PubMed:12853617, ECO:0000269|PubMed:14561886,
CC ECO:0000269|PubMed:14690598, ECO:0000269|PubMed:14729943,
CC ECO:0000269|PubMed:15013450, ECO:0000269|PubMed:15358132,
CC ECO:0000269|PubMed:15967792, ECO:0000269|PubMed:15989963,
CC ECO:0000269|PubMed:16240118, ECO:0000269|PubMed:16373495,
CC ECO:0000269|PubMed:16501073, ECO:0000269|PubMed:16714281,
CC ECO:0000269|PubMed:16885161, ECO:0000269|PubMed:17761681,
CC ECO:0000269|PubMed:18162578, ECO:0000269|PubMed:18443146,
CC ECO:0000269|PubMed:18469165, ECO:0000269|PubMed:18640978,
CC ECO:0000269|PubMed:18676807, ECO:0000269|PubMed:18715869,
CC ECO:0000269|PubMed:19324962, ECO:0000269|PubMed:2076815,
CC ECO:0000269|PubMed:7597069, ECO:0000269|PubMed:7926736,
CC ECO:0000269|PubMed:9315672, ECO:0000269|PubMed:9482746,
CC ECO:0000269|PubMed:9488433, ECO:0000269|PubMed:9685486,
CC ECO:0000269|PubMed:9742129}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Both strand exchange and nuclease activities require magnesium,
CC for the strand exchange activity, calcium can replace magnesium when
CC the linear ds-DNA has been first resected with an exogenous
CC endonuclease.;
CC -!- ACTIVITY REGULATION: 3'-phosphoadenosine 5'-phosphate (pAp) is an
CC inhibitor of KEM1. Sodium-induced GCN4 expression reduces pAp
CC accumulation by activating HAL2 expression, and therefore maintains
CC mRNA degradation capacity which is likely to be important for the
CC accurate and rapid adaptation of gene expression to salt stress.
CC {ECO:0000269|PubMed:16352596}.
CC -!- INTERACTION:
CC P22147; P40070: LSM4; NbExp=3; IntAct=EBI-9642, EBI-188;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
CC Cytoplasm, P-body.
CC -!- DISRUPTION PHENOTYPE: Mutations affect nuclear fusion, leed to reduced
CC chromosome stability and defects in spindle pole body duplication
CC and/or separation as well as loss of viability under conditions of
CC nitrogen starvation. Homozygous diploids are unable to sporulate. Leads
CC also to arrest in pachytene and deficiency in meiotic recombination and
CC sensitivity to oleate. {ECO:0000269|PubMed:17151231,
CC ECO:0000269|PubMed:2027746, ECO:0000269|PubMed:7713413}.
CC -!- MISCELLANEOUS: Present with 11700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the 5'-3' exonuclease family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
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DR EMBL; M90097; AAA35219.1; -; Genomic_DNA.
DR EMBL; X54717; CAA38520.1; -; Genomic_DNA.
DR EMBL; M58367; AAA35036.1; -; Genomic_DNA.
DR EMBL; M36725; AAA35125.1; -; Genomic_DNA.
DR EMBL; X61181; CAA43487.1; -; Genomic_DNA.
DR EMBL; X84705; CAA59180.1; -; Genomic_DNA.
DR EMBL; Z72695; CAA96885.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07940.1; -; Genomic_DNA.
DR PIR; S13743; S13743.
DR RefSeq; NP_011342.1; NM_001181038.1.
DR PDB; 6Q8Y; EM; 3.10 A; z=3-918.
DR PDBsum; 6Q8Y; -.
DR AlphaFoldDB; P22147; -.
DR SMR; P22147; -.
DR BioGRID; 33080; 868.
DR DIP; DIP-656N; -.
DR IntAct; P22147; 119.
DR MINT; P22147; -.
DR STRING; 4932.YGL173C; -.
DR iPTMnet; P22147; -.
DR MaxQB; P22147; -.
DR PaxDb; P22147; -.
DR PRIDE; P22147; -.
DR EnsemblFungi; YGL173C_mRNA; YGL173C; YGL173C.
DR GeneID; 852702; -.
DR KEGG; sce:YGL173C; -.
DR SGD; S000003141; XRN1.
DR VEuPathDB; FungiDB:YGL173C; -.
DR eggNOG; KOG2045; Eukaryota.
DR GeneTree; ENSGT00670000098080; -.
DR HOGENOM; CLU_001581_1_2_1; -.
DR OMA; VASWPWF; -.
DR BioCyc; YEAST:G3O-30661-MON; -.
DR Reactome; R-SCE-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR Reactome; R-SCE-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
DR PRO; PR:P22147; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P22147; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0090512; C:eisosome membrane domain/MCC; IDA:SGD.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000932; C:P-body; IDA:SGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004534; F:5'-3' exoribonuclease activity; IDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0031370; F:eukaryotic initiation factor 4G binding; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000741; P:karyogamy; IEA:UniProtKB-KW.
DR GO; GO:0061157; P:mRNA destabilization; IMP:SGD.
DR GO; GO:0016242; P:negative regulation of macroautophagy; IMP:SGD.
DR GO; GO:0070651; P:nonfunctional rRNA decay; IMP:SGD.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IMP:SGD.
DR GO; GO:0070479; P:nuclear-transcribed mRNA catabolic process, 5'-3' exonucleolytic nonsense-mediated decay; IMP:SGD.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IMP:SGD.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0016075; P:rRNA catabolic process; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR GO; GO:0043144; P:sno(s)RNA processing; IGI:SGD.
DR GO; GO:0006413; P:translational initiation; IMP:SGD.
DR GO; GO:0007089; P:traversing start control point of mitotic cell cycle; IMP:SGD.
DR GO; GO:0016078; P:tRNA catabolic process; IDA:SGD.
DR Gene3D; 2.30.30.30; -; 1.
DR InterPro; IPR027073; 5_3_exoribonuclease.
DR InterPro; IPR016494; 5_3_exoribonuclease_1.
DR InterPro; IPR004859; Put_53exo.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR041385; SH3_12.
DR InterPro; IPR040992; XRN1_D1.
DR InterPro; IPR041106; XRN1_D2_D3.
DR InterPro; IPR040486; Xrn1_D3.
DR InterPro; IPR041412; Xrn1_helical.
DR PANTHER; PTHR12341; PTHR12341; 1.
DR PANTHER; PTHR12341:SF7; PTHR12341:SF7; 1.
DR Pfam; PF18129; SH3_12; 1.
DR Pfam; PF18332; XRN1_D1; 1.
DR Pfam; PF18334; XRN1_D2_D3; 1.
DR Pfam; PF18194; Xrn1_D3; 1.
DR Pfam; PF17846; XRN_M; 1.
DR Pfam; PF03159; XRN_N; 1.
DR PIRSF; PIRSF006743; Exonuclease_Xnr1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Exonuclease; Hydrolase;
KW Karyogamy; Magnesium; Microtubule; Nonsense-mediated mRNA decay; Nuclease;
KW Phosphoprotein; Reference proteome; RNA-binding; rRNA processing.
FT CHAIN 1..1528
FT /note="5'-3' exoribonuclease 1"
FT /id="PRO_0000071395"
FT REGION 1246..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1431..1455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1470..1528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1431..1452
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1474..1516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1506
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MUTAGEN 37
FT /note="N->D: Reduces strongly exonuclease activity."
FT /evidence="ECO:0000269|PubMed:9685486"
FT MUTAGEN 41
FT /note="H->R,D: Reduces strongly exonuclease activity."
FT /evidence="ECO:0000269|PubMed:9685486"
FT MUTAGEN 86
FT /note="D->G: Reduces strongly exonuclease activity."
FT /evidence="ECO:0000269|PubMed:9685486"
FT MUTAGEN 87
FT /note="G->D: Reduces strongly exonuclease activity."
FT /evidence="ECO:0000269|PubMed:9685486"
FT MUTAGEN 93
FT /note="K->M: Reduces strongly exonuclease activity."
FT /evidence="ECO:0000269|PubMed:9685486"
FT MUTAGEN 97
FT /note="Q->E,R: Reduces strongly exonuclease activity."
FT /evidence="ECO:0000269|PubMed:9685486"
FT MUTAGEN 101
FT /note="R->G: Reduces strongly exonuclease activity."
FT /evidence="ECO:0000269|PubMed:9685486"
FT MUTAGEN 176
FT /note="E->G: Reduces strongly exonuclease activity."
FT MUTAGEN 178
FT /note="E->D,G: Reduces strongly exonuclease activity."
FT /evidence="ECO:0000269|PubMed:9685486"
FT MUTAGEN 201
FT /note="C->Y,R: Reduces strongly exonuclease activity."
FT /evidence="ECO:0000269|PubMed:9685486"
FT MUTAGEN 206
FT /note="D->A: Abolishes exonuclease activity in vitro."
FT /evidence="ECO:0000269|PubMed:10454540"
FT MUTAGEN 208
FT /note="D->A: Abolishes exonuclease activity in vitro."
FT /evidence="ECO:0000269|PubMed:10454540"
FT MUTAGEN 592
FT /note="L->P: Reduces strongly exonuclease activity; when
FT associated with Y-710."
FT /evidence="ECO:0000269|PubMed:9685486"
FT MUTAGEN 710
FT /note="Y->C: Reduces strongly exonuclease activity; when
FT associated with P-592."
FT /evidence="ECO:0000269|PubMed:9685486"
FT MUTAGEN 798
FT /note="W->R: Reduces strongly exonuclease activity; when
FT associated with D-1024; F-1043 and P-1197."
FT /evidence="ECO:0000269|PubMed:9685486"
FT MUTAGEN 1024
FT /note="E->D: Reduces strongly exonuclease activity; when
FT associated with R-798; F-1043 and P-1197."
FT /evidence="ECO:0000269|PubMed:9685486"
FT MUTAGEN 1043
FT /note="Y->F: Reduces strongly exonuclease activity; when
FT associated with R-798; D-1024 and P-1197."
FT /evidence="ECO:0000269|PubMed:9685486"
FT MUTAGEN 1197
FT /note="S->P: Reduces strongly exonuclease activity; when
FT associated with R-798; D-1024 and F-1043."
FT /evidence="ECO:0000269|PubMed:9685486"
SQ SEQUENCE 1528 AA; 175460 MW; 49C2EDAF73D3EB92 CRC64;
MGIPKFFRYI SERWPMILQL IEGTQIPEFD NLYLDMNSIL HNCTHGNDDD VTKRLTEEEV
FAKICTYIDH LFQTIKPKKI FYMAIDGVAP RAKMNQQRAR RFRTAMDAEK ALKKAIENGD
EIPKGEPFDS NSITPGTEFM AKLTKNLQYF IHDKISNDSK WREVQIIFSG HEVPGEGEHK
IMNFIRHLKS QKDFNQNTRH CIYGLDADLI MLGLSTHGPH FALLREEVTF GRRNSEKKSL
EHQNFYLLHL SLLREYMELE FKEIADEMQF EYNFERILDD FILVMFVIGN DFLPNLPDLH
LNKGAFPVLL QTFKEALLHT DGYINEHGKI NLKRLGVWLN YLSQFELLNF EKDDIDVEWF
NKQLENISLE GERKRQRVGK KLLVKQQKKL IGSIKPWLME QLQEKLSPDL PDEEIPTLEL
PKDLDMKDHL EFLKEFAFDL GLFITHSKSK GSYSLKMDLD SINPDETEEE FQNRVNSIRK
TIKKYQNAII VEDKEELETE KTIYNERFER WKHEYYHDKL KFTTDSEEKV RDLAKDYVEG
LQWVLYYYYR GCPSWSWYYP HHYAPRISDL AKGLDQDIEF DLSKPFTPFQ QLMAVLPERS
KNLIPPAFRP LMYDEQSPIH DFYPAEVQLD KNGKTADWEA VVLISFVDEK RLIEAMQPYL
RKLSPEEKTR NQFGKDLIYS FNPQVDNLYK SPLGGIFSDI EHNHCVEKEY ITIPLDSSEI
RYGLLPNAKL GAEMLAGFPT LLSLPFTSSL EYNETMVFQQ PSKQQSMVLQ ITDIYKTNNV
TLEDFSKRHL NKVIYTRWPY LRESKLVSLT DGKTIYEYQE SNDKKKFGFI TKPAETQDKK
LFNSLKNSML RMYAKQKAVK IGPMEAIATV FPVTGLVRDS DGGYIKTFSP TPDYYPLQLV
VESVVNEDER YKERGPIPIE EEFPLNSKVI FLGDYAYGGE TTIDGYSSDR RLKITVEKKF
LDSEPTIGKE RLQMDHQAVK YYPSYIVSKN MHLHPLFLSK ITSKFMITDA TGKHINVGIP
VKFEARHQKV LGYARRNPRG WEYSNLTLNL LKEYRQTFPD FFFRLSKVGN DIPVLEDLFP
DTSTKDAMNL LDGIKQWLKY VSSKFIAVSL ESDSLTKTSI AAVEDHIMKY AANIEGHERK
QLAKVPREAV LNPRSSFALL RSQKFDLGDR VVYIQDSGKV PIFSKGTVVG YTTLSSSLSI
QVLFDHEIVA GNNFGGRLRT NRGLGLDASF LLNITNRQFI YHSKASKKAL EKKKQSNNRN
NNTKTAHKTP SKQQSEEKLR KERAHDLLNF IKKDTNEKNS ESVDNKSMGS QKDSKPAKKV
LLKRPAQKSS ENVQVDLANF EKAPLDNPTV AGSIFNAVAN QYSDGIGSNL NIPTPPHPMN
VVGGPIPGAN DVADVGLPYN IPPGFMTHPN GLHPLHPHQM PYPNMNGMSI PPPAPHGFGQ
PISFPPPPPM TNVSDQGSRI VVNEKESQDL KKFINGKQHS NGSTIGGETK NSRKGEIKPS
SGTNSTECQS PKSQSNAADR DNKKDEST
