TY - JOUR AU - Lakatos, Lóránt AU - Groma, Gergely AU - Silhavy, Dániel AU - Nagy, Ferenc István TI - In Arabidopsis thaliana, RNA-Induced Silencing Complex-Loading of MicroRNAs Plays a Minor Regulatory Role During Photomorphogenesis Except for miR163 JF - FRONTIERS IN PLANT SCIENCE J2 - FRONT PLANT SCI VL - 13 PY - 2022 PG - 12 SN - 1664-462X DO - 10.3389/fpls.2022.854869 UR - https://m2.mtmt.hu/api/publication/33039097 ID - 33039097 N1 - Laboratory of Photo and Chronobiology, Biological Research Centre, Institute of Plant Biology, Eötvös Loránd Research Network, Szeged, Hungary Dermatological Research Group, University of Szeged, Szeged, Hungary Export Date: 12 January 2023 Correspondence Address: Lakatos, L.; Laboratory of Photo and Chronobiology, Hungary; email: lakatos.lorant@brc.hu AB - The shift of dark-grown seedlings to the light leads to substantial reprogramming of gene expression, which results in dramatic developmental changes (referred to as de-etiolation or photomorphogenesis). MicroRNAs (miRNAs) regulate most steps of plant development, thus miRNAs might play important role in transcriptional reprogramming during de-etiolation. Indeed, miRNA biogenesis mutants show aberrant de-etiolation. Previous works showed that the total miRNA expression pattern (total miRNAome) is only moderately altered during photomorphogenesis. However, a recent study has shown that plant miRNAs are present in two pools, biologically active miRNAs loaded to RISC (RNA-induced silencing complex-loaded) form while inactive miRNAs accumulate in duplex form upon organ formation. To test if RISC-loading efficiency is changed during photomorphogenesis. we compared the total miRNAome and the RISC-loaded miRNAome of dark-grown and de-etiolated Arabidopsis thaliana seedlings. miRNA sequencing has revealed that although regulated RISC-loading is involved in the control of active miRNAome formation during de-etiolation, this effect is moderate. The total miRNAomes and the RISC-loaded miRNAomes of dark-grown and de-etiolated plants are similar indicating that most miRNAs are loaded onto RISC with similar efficiency in dark and light. Few miRNAs were loaded onto RISC with different efficiency and one miRNA, miR163, was RISC-loaded much more effectively in light than in dark. Thus, our results suggest that although RISC-loading contributes significantly to the control of the formation of organ-specific active miRNA pools, it plays a limited role in the regulation of active miRNA pool formation during de-etiolation. Regulated RISC-loading strongly modifies the expression of miRNA163, could play a role in the fine-tuning of a few other miRNAs, and do not modify the expression of most miRNAs. LA - English DB - MTMT ER - TY - JOUR AU - Szádeczky-Kardoss, István AU - Szaker, Henrik Mihály AU - Verma, Radhika AU - Darkó, Éva AU - Pettkó-Szandtner, Aladár AU - Silhavy, Dániel AU - Csorba, Tibor TI - Elongation factor TFIIS is essential for heat stress adaptation in plants JF - NUCLEIC ACIDS RESEARCH J2 - NUCLEIC ACIDS RES VL - 50 PY - 2022 IS - 4 SP - 1927 EP - 1950 PG - 24 SN - 0305-1048 DO - 10.1093/nar/gkac020 UR - https://m2.mtmt.hu/api/publication/32640714 ID - 32640714 N1 - Funding Agency and Grant Number: Hungarian Academy of SciencesHungarian Academy of Sciences; Tempus Public Foundation; Hungarian Scientific Research FundOrszagos Tudomanyos Kutatasi Alapprogramok (OTKA) [K-129283, K-137722, K-136513, K-139349]; Hungarian ScientificResearch FundOrszagos Tudomanyos Kutatasi Alapprogramok (OTKA) [K-129283] Funding text: Hungarian Academy of Sciences [to T.C.]; Tempus Public Foundation [to R.V.]; Hungarian Scientific Research Fund [K-129283, K-137722, K-136513 and K-139349]. Funding for open access charge: Hungarian ScientificResearch Fund [K-129283]. LA - English DB - MTMT ER - TY - JOUR AU - Auth, Mariann AU - Nyikó, Tünde AU - Auber, Andor AU - Silhavy, Dániel TI - The role of RST1 and RIPR proteins in plant RNA quality control systems JF - PLANT MOLECULAR BIOLOGY J2 - PLANT MOL BIOL VL - 106 PY - 2021 IS - 3 SP - 271 EP - 284 PG - 14 SN - 0167-4412 DO - 10.1007/s11103-021-01145-9 UR - https://m2.mtmt.hu/api/publication/31997619 ID - 31997619 AB - To keep mRNA homeostasis, the RNA degradation, quality control and silencing systems should act in balance in plants. Degradation of normal mRNA starts with deadenylation, then deadenylated transcripts are degraded by the SKI-exosome 3 '-5 ' and/or XRN4 5 '-3 ' exonucleases. RNA quality control systems identify and decay different aberrant transcripts. RNA silencing degrades double-stranded transcripts and homologous mRNAs. It also targets aberrant and silencing prone transcripts. The SKI-exosome is essential for mRNA homeostasis, it functions in normal mRNA degradation and different RNA quality control systems, and in its absence silencing targets normal transcripts. It is highly conserved in eukaryotes, thus recent reports that the plant SKI-exosome is associated with RST1 and RIPR proteins and that, they are required for SKI-exosome-mediated decay of silencing prone transcripts were unexpected. To clarify whether RST1 and RIPR are essential for all SKI-exosome functions or only for the elimination of silencing prone transcripts, degradation of different reporter transcripts was studied in RST1 and RIPR inactivated Nicotiana benthamiana plants. As RST1 and RIPR, like the SKI-exosome, were essential for Non-stop and No-go decay quality control systems, and for RNA silencing- and minimum ORF-mediated decay, we propose that RST1 and RIPR are essential components of plant SKI-exosome supercomplex. Key message The RST1 and RIPR proteins are required for the degradation of aberrant transcripts lacking a stop codon and the 5 ' cleavage fragments of no-go decay, RNA silencing and minimum ORF. LA - English DB - MTMT ER - TY - JOUR AU - Kurilla, Anita AU - Szőke, Anita AU - Auber, Andor AU - Káldi, Krisztina AU - Silhavy, Dániel TI - Expression of the translation termination factor eRF1 is autoregulated by translational readthrough and 3'UTR intron-mediated NMD inNeurospora crassa JF - FEBS LETTERS J2 - FEBS LETT VL - 594 PY - 2020 IS - 21 SP - 3504 EP - 3517 PG - 14 SN - 0014-5793 DO - 10.1002/1873-3468.13918 UR - https://m2.mtmt.hu/api/publication/31612927 ID - 31612927 N1 - Funding Agency and Grant Number: Biological Research Center; SZBK [Ginop-00001]; NKFIH OTKAOrszagos Tudomanyos Kutatasi Alapprogramok (OTKA) [K129177, K116963, K115953, K132393]; NKFIH OTKA (FIKP 2019); UNKP; IKOM [Ginop-00015] Funding text: Open access funding provided by Biological Research Center. We are grateful to M. Peline Toth for technical assistances (Agricultural Biotechnology Institute). Research was supported by the SZBK Ginop-00001 and the NKFIH OTKA grants for DS (K129177, K116963) and KK (K115953, K132393, FIKP 2019). A. Kurilla and A. Auber are graduate students of the ELTE 'Classical and Molecular Genetics' Ph.D. program, A. Szoke is a student of the Molecular Medicine PhD School of Semmelweis University. A. Kurilla and A. Szoke were also supported by the UNKP. DS was supported by the IKOM Ginop-00015. AB - Eukaryotic release factor 1 (eRF1) is a translation termination factor that binds to the ribosome at stop codons. The expression of eRF1 is strictly controlled, since its concentration defines termination efficiency and frequency of translational readthrough. Here, we show that eRF1 expression inNeurospora crassais controlled by an autoregulatory circuit that depends on the specific 3'UTR structure oferf1mRNA. The stop codon context oferf1promotes readthrough that protects the mRNA from its 3'UTR-induced nonsense-mediated mRNA decay (NMD). High eRF1 concentration leads to inefficient readthrough, thereby allowing NMD-mediatederf1degradation. We propose that eRF1 expression is controlled by similar autoregulatory circuits in many fungi and seed plants and discuss the evolution of autoregulatory systems of different translation termination factors. LA - English DB - MTMT ER - TY - JOUR AU - Jánosi, Imre Miklós AU - Silhavy, Dániel AU - Tamás, Júlia AU - Csontos, Péter TI - Bulbous perennials precisely detect the length of winter and adjust flowering dates JF - NEW PHYTOLOGIST J2 - NEW PHYTOL VL - 228 PY - 2020 IS - 5 SP - 1535 EP - 1547 PG - 13 SN - 0028-646X DO - 10.1111/nph.16740 UR - https://m2.mtmt.hu/api/publication/31386132 ID - 31386132 N1 - Department of Physics of Complex Systems, Eötvös Loránd University, Pázmány Péter sétány 1/A, Budapest, H-1117, Hungary Max Planck Institute for the Physics of Complex Systems, Nöthnitzer Str. 38, Dresden, 01187, Germany Biological Research Centre, Temesvári krt. 62, Szeged, H-6726, Hungary Department of Botany, Hungarian Natural History Museum, Könyves Kálmán krt. 40, Budapest, H-1089, Hungary Institute for Soil Science and Agricultural Chemistry, Centre for Agricultural Research, Herman Ottó u. 15, Budapest, H-1022, Hungary Cited By :1 Export Date: 20 April 2021 CODEN: NEPHA Correspondence Address: Jánosi, I.M.; Department of Physics of Complex Systems, Pázmány Péter sétány 1/A, Hungary; email: imre.janosi@ttk.elte.hu Correspondence Address: Jánosi, I.M.; Max Planck Institute for the Physics of Complex Systems, Nöthnitzer Str. 38, Germany; email: imre.janosi@ttk.elte.hu LA - English DB - MTMT ER - TY - JOUR AU - Sulkowska, Aleksandra AU - Auber, Andor AU - Sikorski, Pawel J. AU - Silhavy, Dániel AU - Auth, Mariann AU - Sitkiewicz, Ewa AU - Jean, Viviane AU - Merret, Remy AU - Bousquet-Antonelli, Cecile AU - Kufel, Joanna TI - RNA Helicases from the DEA(D/H)-Box Family Contribute to Plant NMD Efficiency JF - PLANT AND CELL PHYSIOLOGY J2 - PLANT CELL PHYSIOL VL - 61 PY - 2020 IS - 1 SP - 144 EP - 157 PG - 14 SN - 0032-0781 DO - 10.1093/pcp/pcz186 UR - https://m2.mtmt.hu/api/publication/31281263 ID - 31281263 N1 - Funding Agency and Grant Number: National Science Centre [UMO-2012/05/D/NZ1/00030, UMO2014/15/B/NZ2/02302, UMO2018/28/T/NZ1/00077, UMO-2015/19/N/NZ2/00200]; EMBO Short-Term FellowshipEuropean Molecular Biology Organization (EMBO) [ASTF-396-2015, STF-7351]; Agence Nationale de la RechercheFrench National Research Agency (ANR) [ANR-14-CE10-0015, ANR3'ModRN: ANR-15-CE12-0008-12]; National Research, Development and Innovation Office [NKFIH K-129177, K-116963]; European Union-the European Regional Development Fund Innovative economy 2007-13 [POIG.02.02.00-14-024/08-00S] Funding text: National Science Centre [UMO-2012/05/D/NZ1/00030], [UMO2014/15/B/NZ2/02302] to J.K.; National Science Centre [UMO2018/28/T/NZ1/00077], [UMO-2015/19/N/NZ2/00200] and EMBO Short-Term Fellowship [ASTF-396-2015], [STF-7351] to A. S.; Agence Nationale de la Recherche [ANR-14-CE10-0015], [ANR3'ModRN: ANR-15-CE12-0008-12] to C.B.-A.; and National Research, Development and Innovation Office [NKFIH-K 129177] to D.S. Experiments were carried out with the use of CePT infrastructure financed by the European Union-the European Regional Development Fund Innovative economy 2007-13 [AGREEMENT POIG.02.02.00-14-024/08-00S]. National Research, Development and Innovation Office [NKFIH K-129177, K-116963]. Institute of Genetics and Biotechnology, Faculty of Biology, University of Warsaw, Pawinskiego 5a, Warsaw, 02-106, Poland Agricultural Biotechnology Institute, Szent-Györgyi 4, Gödöllo, H-2100, Hungary Proteomics Laboratory, Biophysics Department, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawinskiego 5a, Warszawa, 02-106, Poland UMR5096 LGDP, Universite de Perpignan Via Domitia, UMR5096 LGDP58, Avenue Paul Alduy, Perpignan Cedex, 66860, France CNRS, UMR5096 LGDP, Perpignan Cedex, France Centre of New Technologies, University OfWarsaw, Banacha 2c, Warsawz, 02-097, Poland Biological Research Centre, Hungarian Academy of Sciences, Institute of Plant Biology, Temesvari krt. 62, Szeged, H-6726, Hungary Cited By :3 Export Date: 9 September 2020 CODEN: PCPHA Correspondence Address: Kufel, J.; Institute of Genetics and Biotechnology, Faculty of Biology, University of Warsaw, Pawinskiego 5a, Poland; email: kufel@ibb.waw.pl Institute of Genetics and Biotechnology, Faculty of Biology, University of Warsaw, Pawinskiego 5a, Warsaw, 02-106, Poland Agricultural Biotechnology Institute, Szent-Györgyi 4, Gödöllo, H-2100, Hungary Proteomics Laboratory, Biophysics Department, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawinskiego 5a, Warszawa, 02-106, Poland UMR5096 LGDP, Universite de Perpignan Via Domitia, UMR5096 LGDP58, Avenue Paul Alduy, Perpignan Cedex, 66860, France CNRS, UMR5096 LGDP, Perpignan Cedex, France Centre of New Technologies, University OfWarsaw, Banacha 2c, Warsawz, 02-097, Poland Biological Research Centre, Hungarian Academy of Sciences, Institute of Plant Biology, Temesvari krt. 62, Szeged, H-6726, Hungary Cited By :5 Export Date: 28 May 2021 CODEN: PCPHA Correspondence Address: Kufel, J.; Institute of Genetics and Biotechnology, Pawinskiego 5a, Poland; email: kufel@ibb.waw.pl AB - Nonsense-mediated mRNA decay (NMD) is a conserved eukaryotic RNA surveillance mechanism that degrades aberrantm RNAs comprising a premature translation termination codon. The adenosine triphosphate (ATP)-dependent RNA helicase up-frameshift 1 (UPF1) is a major NMD factor in all studied organisms; however, the complexity of this mechanism has not been fully characterized in plants. To identify plant NMD factors, we analyzed UPF1-interacting proteins using tandem affinity purification coupled to mass spectrometry.Canonical members of the NMD pathway were found along with numerous NMD candidate factors, including conserved DEA(D/H)-box RNA helicase homologs of human DDX3, DDX5 and DDX6, translation initiation factors, ribosomal proteins and transport factors. Our functional studies revealed that depletion of DDX3 helicases enhances the accumulation of NMD target reporterm RNAs but does not result in increased protein levels. In contrast, silencing of DDX6 group leads to decreased accumulation of the NMD substrate. The inhibitory effect of DDX6-like helicases on NMD was confirmed by transient over-expression of RH12 helicase. These results indicate that DDX3 and DDX6 helicases in plants have a direct and opposing contribution to NMD and act as functional NMD factors. LA - English DB - MTMT ER - TY - JOUR AU - Kurilla, Anita AU - Tóth, Tímea AU - Dorgai, L. AU - Darula, Zsuzsanna AU - Lakatos, Tamás AU - Silhavy, Dániel AU - Kerényi, Zoltán AU - Dallmann, G. TI - Nectar- and stigma exudate-specific expression of an acidic chitinase could partially protect certain apple cultivars against fire blight disease JF - PLANTA J2 - PLANTA VL - 251 PY - 2020 IS - 1 SN - 0032-0935 DO - 10.1007/s00425-019-03303-2 UR - https://m2.mtmt.hu/api/publication/30982110 ID - 30982110 N1 - Agricultural Biotechnology Institute, Szent-Györgyi 4, Gödöllő, 2100, Hungary Research Institute for Fruitgrowing and Ornamentals, Park 2, Budapest, 1223, Hungary Biocenter Ltd, Temesvári 62, Szeged, 6726, Hungary Biological Research Centre, Hungarian Academy of Sciences, Temesvári krt 62, Szeged, 6726, Hungary MTKI, Lucsony 24, Mosonmagyaróvár, 9200, Hungary Export Date: 11 December 2019 CODEN: PLANA Correspondence Address: Silhavy, D.; Biological Research Centre, Hungarian Academy of Sciences, Temesvári krt 62, Hungary; email: silhavy@brc.hu Funding Agency and Grant Number: MTA Biological Research Center (MTA SZBK); OTKAOrszagos Tudomanyos Kutatasi Alapprogramok (OTKA) [K129177, K116963] Funding text: Open access funding provided by MTA Biological Research Center (MTA SZBK). We are grateful to M. Peline Toth, M. Csanyi and J. Nadudvarine Novak for transformations and various technical assistances. We thank A. Kerekes (Agricultural Biotechnology Institute) for the anti-Machi3-1 antibody and A. Auber (Agricultural Biotechnology Institute) for his help with the bioinformatical studies and Z. K. Varga for his help in statistical analyses. We are especially grateful to E. Van de Weg (Wageningen, Netherlands) for the M. floribunda 821 DNA samples. We thank A. Hegedus (Szent Istvan University, Hungary) for the useful comments about the manuscript. Research was supported by grants from the OTKA (K129177, K116963). A. Kurilla is a graduate student of ELTE "Classical and Molecular Genetics" Ph.D. program. Agricultural Biotechnology Institute, Szent-Györgyi 4, Gödöllő, 2100, Hungary Research Institute for Fruitgrowing and Ornamentals, Park 2, Budapest, 1223, Hungary Biocenter Ltd, Temesvári 62, Szeged, 6726, Hungary Biological Research Centre, Hungarian Academy of Sciences, Temesvári krt 62, Szeged, 6726, Hungary MTKI, Lucsony 24, Mosonmagyaróvár, 9200, Hungary Cited By :1 Export Date: 9 September 2020 CODEN: PLANA Correspondence Address: Silhavy, D.; Biological Research Centre, Hungarian Academy of Sciences, Temesvári krt 62, Hungary; email: silhavy@brc.hu LA - English DB - MTMT ER - TY - JOUR AU - Auber, Andor AU - Nyikó, Tünde AU - Merai, Zsuzsanna AU - Silhavy, Dániel TI - Characterization of Eukaryotic Release Factor 3 (eRF3) Translation Termination Factor in Plants JF - PLANT MOLECULAR BIOLOGY REPORTER J2 - PLANT MOL BIOL REP VL - 36 PY - 2018 IS - 5-6 SP - 858 EP - 869 PG - 12 SN - 0735-9640 DO - 10.1007/s11105-018-1128-5 UR - https://m2.mtmt.hu/api/publication/30450590 ID - 30450590 N1 - Department of Genetics, Agricultural Biotechnology Institute, Gödöllő, H-2100, Hungary Gregor Mendel Institute, Austrian Academy of Sciences, Dr. Bohr-Gasse 3, Vienna, 1030, Austria Export Date: 9 September 2020 Correspondence Address: Silhavy, D.; Department of Genetics, Agricultural Biotechnology InstituteHungary; email: silhavy.daniel@abc.naik.hu AB - Eukaryotic translation termination is mediated by two conserved interacting release factors, eRF1 and eRF3. eRF1 recognizes the stop codon and promotes the hydrolysis of the polypeptide chain, while eukaryotic eRF3 stimulates eRF1 release activity in the presence of GTP. It is widely believed that translation termination is highly conserved in eukaryotes. However, recent results that eRF1 is present in multiple, partially redundant copies in plants and that eRF1 expression is controlled by a complex, plant-specific autoregulatory circuit suggest that regulation of translation termination might be especially complex in plants. Surprisingly, very little is known about translation termination in plant, for instance, the eRF3 termination factor has not been analyzed in plants yet. Thus, we wanted to identify and characterize the eRF3 translation termination factor in plants. By combining a range of transient and transgenic assay here, we identified plant eRF3 and showed that it directly interacts with eRF1. In contrast to eRF1, plant eRF3 is not autoregulated, while eRF3 and eRF1 expressions are connected. We also demonstrated that eRF3 interacts with the core NMD factor, UPF1, and the expression of eRF3 is NMD regulated in certain plant species suggesting that in addition to the normal translation termination, eRF3 could be connected to plant nonsense-mediated decay (NMD). Finally, it appears that the plant termination factors are present in physiologically different concentrations, while eRF1 concentration limits the efficiency of both translation termination and NMD, eRF3 is present in non-limiting concentration. LA - English DB - MTMT ER - TY - JOUR AU - Szádeczky-Kardoss, István AU - Gal, L AU - Auber, Andor AU - Taller, János AU - Silhavy, Dániel TI - The No-go decay system degrades plant mRNAs that contain a long A-stretch in the coding region JF - PLANT SCIENCE J2 - PLANT SCI VL - 275 PY - 2018 SP - 19 EP - 27 PG - 9 SN - 0168-9452 DO - 10.1016/j.plantsci.2018.07.008 UR - https://m2.mtmt.hu/api/publication/3420895 ID - 3420895 N1 - : IRELAND Agricultural Biotechnology Institute, Szent-Györgyi 4, Gödöllő, H-2100, Hungary University Pannonia Georgikon, Festetics 7, Keszthely, 8360, Hungary Cited By :12 Export Date: 9 September 2020 CODEN: PLSCE Correspondence Address: Silhavy, D.; Agricultural Biotechnology Institute, Szent-Györgyi 4, Hungary; email: silhavy@abc.hu AB - RNA quality control systems identify and degrade aberrant mRNAs, thereby preventing the accumulation of faulty proteins. Non-stop decay (NSD) and No-go decay (NGD) are closely related RNA quality control systems that act during translation. NSD degrades mRNAs lacking a stop codon, while NGD recognizes and decays mRNAs that contain translation elongation inhibitory structures. NGD has been intensively studied in yeast and animals but it has not been described in plants yet. In yeast, NGD is induced if the elongating ribosome is stalled by a strong inhibitory structure. Then, the mRNA is cleaved by an unknown nuclease and the cleavage fragments are degraded. Here we show that NGD also operates in plant. We tested several potential NGD cis-elements and found that in plants, unlike in yeast, only long A-stretches induce NGD. These long A-stretches trigger endonucleolytic cleavage, and then the 5' fragments are degraded in a Pelota-, HBS1- and SKI2- dependent manner, while XRN4 eliminates the 3' fragment. We also show that plant NGD operates gradually, the longer the A stretch, the more efficient the cleavage. Our data suggest that mechanistically NGD is conserved in eukaryotes, although the NGD inducing cis-elements could be different. Moreover, we found that Arabidopsis AtPelota1 functions in both NGD and NSD, while AtPelota2 represses these quality control systems. The function of plant NGD will be discussed. LA - English DB - MTMT ER - TY - JOUR AU - Szádeczky-Kardoss, István AU - Csorba, Tibor AU - Auber, Andor AU - Schamberger, Anita AU - Nyikó, Tünde AU - Taller, János AU - Orbán, Tamás I. AU - Burgyán, József AU - Silhavy, Dániel TI - The nonstop decay and the RNA silencing systems operate cooperatively in plants JF - NUCLEIC ACIDS RESEARCH J2 - NUCLEIC ACIDS RES VL - 46 PY - 2018 IS - 9 SP - 4632 EP - 4648 PG - 17 SN - 0305-1048 DO - 10.1093/nar/gky279 UR - https://m2.mtmt.hu/api/publication/3370402 ID - 3370402 N1 - Agricultural Biotechnology Institute, Szent-Györgyi 4, Gödöllö, H-2100, Hungary Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Magyar tudósok körútja 2, Budapest, 1117, Hungary University Pannonia Georgikon, Festetics 7, Keszthely, 8360, Hungary Cited By :27 Export Date: 28 May 2021 CODEN: NARHA Correspondence Address: Silhavy, D.; Agricultural Biotechnology Institute, Szent-Györgyi 4, Hungary; email: silhavy.daniel@abc.naik.hu AB - Translation-dependent mRNA quality control systems protect the protein homeostasis of eukaryotic cells by eliminating aberrant transcripts and stimulating the decay of their protein products. Although these systems are intensively studied in animals, little is known about the translation-dependent quality control systems in plants. Here, we characterize the mechanism of nonstop decay (NSD) system in Nicotiana benthamiana model plant. We show that plant NSD efficiently degrades nonstop mRNAs, which can be generated by premature polyadenylation, and stop codon-less transcripts, which are produced by endonucleolytic cleavage. We demonstrate that in plants, like in animals, Pelota, Hbs1 and SKI2 proteins are required for NSD, supporting that NSD is an ancient and conserved eukaryotic quality control system. Relevantly, we found that NSD and RNA silencing systems cooperate in plants. Plant silencing predominantly represses target mRNAs through endonucleolytic cleavage in the coding region. Here we show that NSD is required for the elimination of 5' cleavage product of mi- or siRNA-guided silencing complex when the cleavage occurs in the coding region. We also show that NSD and nonsense-mediated decay (NMD) quality control systems operate independently in plants. LA - English DB - MTMT ER -