TY - JOUR AU - Tornyi, Ilona AU - Lazar, Jozsef AU - Pettkó-Szandtner, Aladár AU - Hunyadi-Gulyás Éva, Csilla AU - Takács, László Kristóf TI - Epitomics: Analysis of Plasma C9 Epitope Heterogeneity in the Plasma of Lung Cancer Patients and Control Subjects JF - INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES J2 - INT J MOL SCI VL - 24 PY - 2023 IS - 18 PG - 13 SN - 1661-6596 DO - 10.3390/ijms241814359 UR - https://m2.mtmt.hu/api/publication/34154576 ID - 34154576 AB - The human proteome is more complex than the genetic code predicts it to be. Epitomics, or protein epitome profiling, is a tool for understanding sub-protein level variation. With the ultimate goal to explore C9 proteoforms and their relevance to lung cancer, here we report plasma C9 epitope-associated molecular heterogeneity in plasma samples of lung cancer patients and control subjects. We show three C9 epitopes (BSI0449, BSI0581, BSI0639) with markedly different association with lung cancer (“unaltered”, “upregulated” and “downregulated”). In order to exclude confounding effects, we show first that the three epitope-defining mAbs recognize C9 in purified form and in the natural context, in the human plasma. Then, we present data demonstrating the lack of major epitope interdependence or overlap. The next experiments represent a quest toward the understanding of the molecular basis of apparent disparate association with lung cancer. Using immunochemistry, SDS PAGE and LC-MS/MS technologies, we demonstrate that epitope-specific immunoprecipitates of plasma C9 seem identical regarding peptide sequence. However, we found epitope-specific posttranslational modification and coprecipitated protein composition differences with respect to control and lung cancer plasma. Epitope profiling enabled the classification of hypothetical C9 proteoforms through differential association with lung cancer. LA - English DB - MTMT ER - TY - JOUR AU - Ughy, Bettina AU - Nagyapáti, Sarolta AU - Lajkó, Dézi Bianka AU - Letoha, Tamas AU - Prohaszka, Adam AU - Deeb, Dima AU - Dér, András AU - Pettkó-Szandtner, Aladár AU - Szilák, László TI - Reconsidering Dogmas about the Growth of Bacterial Populations JF - CELLS J2 - CELLS-BASEL VL - 12 PY - 2023 IS - 10 PG - 15 SN - 2073-4409 DO - 10.3390/cells12101430 UR - https://m2.mtmt.hu/api/publication/33846356 ID - 33846356 N1 - Funding Agency and Grant Number: Hungarian Ministry for National Economy and National Research Development and Innovation Office of Hungary [GINOP-2.3.2-15-2016-00058]; European Union [101000501] Funding text: This research was funded by grants of the Hungarian Ministry for National Economy and National Research Development and Innovation Office of Hungary (GINOP-2.3.2-15-2016-00058) and the European Unions Horizon 2020 Research and Innovation Program under grant agreement No 101000501. AB - The growth of bacterial populations has been described as a dynamic process of continuous reproduction and cell death. However, this is far from the reality. In a well fed, growing bacterial population, the stationary phase inevitably occurs, and it is not due to accumulated toxins or cell death. A population spends the most time in the stationary phase, where the phenotype of the cells alters from the proliferating ones, and only the colony forming unit (CFU) decreases after a while, not the total cell concentration. A bacterial population can be considered as a virtual tissue as a result of a specific differentiation process, in which the exponential-phase cells develop to stationary-phase cells and eventually reach the unculturable form. The richness of the nutrient had no effect on growth rate or on stationary cell density. The generation time seems not to be a constant value, but it depended on the concentration of the starter cultures. Inoculations with serial dilutions of stationary populations reveal a so-called minimal stationary cell concentration (MSCC) point, up to which the cell concentrations remain constant upon dilutions; that seems to be universal among unicellular organisms. LA - English DB - MTMT ER - TY - JOUR AU - Hudák, Anett AU - Roach, Matthew AU - Pusztai, Dávid AU - Pettkó-Szandtner, Aladár AU - Letoha, Annamária AU - Szilák, László AU - Azzouz, Mimoun AU - Letoha, Tamás TI - Syndecan-4 Mediates the Cellular Entry of Adeno-Associated Virus 9 JF - INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES J2 - INT J MOL SCI VL - 24 PY - 2023 IS - 4 PG - 17 SN - 1661-6596 DO - 10.3390/ijms24043141 UR - https://m2.mtmt.hu/api/publication/33630992 ID - 33630992 N1 - Export Date: 26 April 2023 AB - Due to their low pathogenicity, immunogenicity, and long-term gene expression, adeno-associated virus (AAV) vectors emerged as safe and efficient gene delivery tools, over-coming setbacks experienced with other viral gene delivery systems in early gene therapy trials. Among AAVs, AAV9 can translocate through the blood-brain barrier (BBB), making it a promising gene delivery tool for transducing the central nervous system (CNS) via systemic administration. Recent reports on the shortcomings of AAV9-mediated gene delivery into the CNS require reviewing the molecular base of AAV9 cellular biology. A more detailed understanding of AAV9’s cellular entry would eradicate current hurdles and enable more efficient AAV9-based gene therapy approaches. Syndecans, the transmembrane family of heparan-sulfate proteoglycans, facilitate the cellular uptake of various viruses and drug delivery systems. Utilizing human cell lines and syndecan-specific cellular assays, we assessed the involvement of syndecans in AAV9’s cellular entry. The ubiquitously expressed isoform, syndecan-4 proved its superiority in facilitating AAV9 internalization among syndecans. Introducing syndecan-4 into poorly transducible cell lines enabled robust AAV9-dependent gene transduction, while its knockdown reduced AAV9’s cellular entry. Attachment of AAV9 to syndecan-4 is mediated not just by the polyanionic heparan-sulfate chains but also by the cell-binding domain of the extracellular syndecan-4 core protein. Co-immunoprecipitation assays and affinity proteomics also confirmed the role of syndecan-4 in the cellular entry of AAV9. Overall, our findings highlight the universally expressed syndecan-4 as a significant contributor to the cellular internalization of AAV9 and provide a molecular-based, rational explanation for the low gene delivery potential of AAV9 into the CNS. LA - English DB - MTMT ER - TY - JOUR AU - ZHANG, Senlei AU - Wang, Ting AU - Lima, Rui AU - Pettkó-Szandtner, Aladár AU - Kereszt, Attila AU - Downie, J. Allan AU - Kondorosi, Éva TI - Widely conserved AHL transcription factors are essential for NCR gene expression and nodule development in Medicago JF - NATURE PLANTS J2 - NAT PLANTS VL - 9 PY - 2023 IS - 2 SP - 280 EP - 288 PG - 9 SN - 2055-026X DO - 10.1038/s41477-022-01326-4 UR - https://m2.mtmt.hu/api/publication/33560404 ID - 33560404 N1 - Funding Agency and Grant Number: International Balzan Foundation; Hungarian National Research, Development and Innovation Office [K128486]; Hungarian Academy of Sciences; China Scholarship Council fellowship; Frontline Research project [KKP129924] Funding text: We thank X. Li from the Huazhong Agricultural University for providing seeds of G. max cv. Williams 82 and for providing aid with the screening of target proteins in soybean. This work was supported by the Frontline Research project (KKP129924) and the Balzan Prize (2018) from the International Balzan Foundation to E.K.; OTKA grant (K128486) from the Hungarian National Research, Development and Innovation Office to A.K.; a visiting fellowship from the Hungarian Academy of Sciences to J. A. D; and the China Scholarship Council fellowship to S.Z. and T.W. AB - Symbiotic nitrogen fixation by Rhizobium bacteria in the cells of legume root nodules alleviates the need for nitrogen fertilizers. Nitrogen fixation requires the endosymbionts to differentiate into bacteroids which can be reversible or terminal. The latter is controlled by the plant, it is more beneficial and has evolved in multiple clades of the Leguminosae family. The plant effectors of terminal differentiation in inverted repeat-lacking clade legumes (IRLC) are nodule-specific cysteine-rich (NCR) peptides, which are absent in legumes such as soybean where there is no terminal differentiation of rhizobia. It was assumed that NCR s co-evolved with specific transcription factors, but our work demonstrates that expression of NCR genes does not require NCR -specific transcription factors. Introduction of the Medicago truncatula NCR169 gene under its own promoter into soybean roots resulted in its nodule-specific expression, leading to bacteroid changes associated with terminal differentiation. We identified two AT-Hook Motif Nuclear Localized (AHL) transcription factors from both M. truncatula and soybean nodules that bound to AT-rich sequences in the NCR169 promoter inducing its expression. Whereas mutation of NCR169 arrested bacteroid development at a late stage, the absence of MtAHL1 or MtAHL2 completely blocked bacteroid differentiation indicating that they also regulate other NCR genes required for the development of nitrogen-fixing nodules. Regulation of NCR s by orthologous transcription factors in non-IRLC legumes opens up the possibility of increasing the efficiency of nitrogen fixation in legumes lacking NCR s. LA - English DB - MTMT ER - TY - JOUR AU - Márton, Margita AU - Bánhegyi, Gábor AU - Gyöngyösi, Norbert AU - Kálmán, Eszter Éva AU - Pettkó-Szandtner, Aladár AU - Káldi, Krisztina AU - Kapuy, Orsolya TI - A systems biological analysis of the ATF4-GADD34-CHOP regulatory triangle upon endoplasmic reticulum stress JF - FEBS OPEN BIO J2 - FEBS OPEN BIO VL - 12 PY - 2022 IS - 11 SP - 2065 EP - 2082 PG - 18 SN - 2211-5463 DO - 10.1002/2211-5463.13484 UR - https://m2.mtmt.hu/api/publication/33127391 ID - 33127391 N1 - Department of Molecular Biology at the Institute of Biochemistry and Molecular Biology, Semmelweis University, Budapest, Hungary Laboratory of Proteomics Research, Biological Research Centre, Szeged, Hungary Department of Physiology, Semmelweis University, Budapest, Hungary Cited By :3 Export Date: 25 October 2023 Correspondence Address: Kapuy, O.; O. Kapuy, Hungary; email: kapuy.orsolya@med.semmelweis-univ.hu Chemicals/CAS: guanabenz, 5051-62-7; thapsigargin, 67526-95-8 Funding details: GINOP‐2.3.2‐15‐2016‐00032 Funding details: 739593 Funding details: Semmelweis Egyetem Funding details: Emberi Eroforrások Minisztériuma, EMMI, ÚNKP-22-4-II-SE-20 Funding details: Nemzeti Kutatási, Fejlesztési és Innovaciós Alap, NKFIA, EFOP‐3.6.3‐VEKOP‐16‐2017‐00009, FK 132474, FK 134267, K 132393 Funding text 1: The work was financially supported by the National Research, Development and Innovation Fund of Hungary under Grant FK 134267 (OK), Grant FK 132474 (NG), Grant K 132393 (KK), EFOP‐3.6.3‐VEKOP‐16‐2017‐00009 (MM), and by the New National Excellence Program of the Ministry of Human Capacities ÚNKP‐22‐4‐II‐SE‐20 (MM). We thank the Single Cell Omics Advanced Core Facility staff of the HCEMM and Biological Research Center for help with their resources and their support. HCEMM has received funding from the EU's Horizon 2020 research and innovation program under grant agreement No. 739593. AP‐S was supported by the Development and Innovation Office of Hungary (GINOP‐2.3.2‐15‐2016‐00032). We are thankful for the technical support of Krisztina Percze and Dániel Fodor (Semmelweis University, Hungary). We thank Peter Baker for the development and maintenance, and the ELKH Cloud ( https://science‐cloud.hu/ ) for hosting the ProteinProspector search engine. Funding text 2: The work was financially supported by the National Research, Development and Innovation Fund of Hungary under Grant FK 134267 (OK), Grant FK 132474 (NG), Grant K 132393 (KK), EFOP-3.6.3-VEKOP-16-2017-00009 (MM), and by the New National Excellence Program of the Ministry of Human Capacities ÚNKP-22-4-II-SE-20 (MM). We thank the Single Cell Omics Advanced Core Facility staff of the HCEMM and Biological Research Center for help with their resources and their support. HCEMM has received funding from the EU's Horizon 2020 research and innovation program under grant agreement No. 739593. AP-S was supported by the Development and Innovation Office of Hungary (GINOP-2.3.2-15-2016-00032). We are thankful for the technical support of Krisztina Percze and Dániel Fodor (Semmelweis University, Hungary). We thank Peter Baker for the development and maintenance, and the ELKH Cloud (https://science-cloud.hu/) for hosting the ProteinProspector search engine. AB - Endoplasmic reticulum (ER) stress-dependent accumulation of incorrectly folded proteins leads to activation of the unfolded protein response. The role of the unfolded protein response (UPR) is to avoid cell damage and restore the homeostatic state by autophagy; however, excessive ER stress results in apoptosis. Here we investigated the ER stress-dependent feedback loops inside one of the UPR branches by focusing on PERK-induced ATF4 and its two targets, called CHOP and GADD34. Our goal was to qualitatively describe the dynamic behavior of the system by exploring the key regulatory motifs using both molecular and theoretical biological techniques. Using the HEK293T cell line as a model system, we confirmed that the life-or-death decision is strictly regulated. We investigated the dynamic characteristics of the crucial elements of the PERK pathway at both the RNA and protein level upon tolerable and excessive levels of ER stress. Of particular note, inhibition of GADD34 or CHOP resulted in various phenotypes upon high levels of ER stress. Our computer simulations suggest the existence of two new feedback loops inside the UPR. First, GADD34 seems to have a positive effect on ATF4 activity, while CHOP inhibits it. We claim that these newly described feedback loops ensure the fine-tuning of the ATF4-dependent stress response mechanism of the cell. © 2022 The Authors. FEBS Open Bio published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies. LA - English DB - MTMT ER - TY - JOUR AU - Wisniewski, Éva AU - Czárán, Domonkos Tamás AU - Kovács, Fanni AU - Bahurek, Enikő AU - Németh, Afrodité AU - Sasvári, Péter AU - Szanda, Gergő AU - Pettkó-Szandtner, Aladár AU - Klement, Éva AU - Ligeti, Erzsébet AU - Csépányi-Kömi, Roland TI - A Novel BRET-Based GAP assay reveals phosphorylation-dependent regulation of the RAC-specific GTPase activating protein ARHGAP25 JF - FASEB JOURNAL J2 - FASEB J VL - 36 PY - 2022 IS - 11 PG - 19 SN - 0892-6638 DO - 10.1096/fj.202200689R UR - https://m2.mtmt.hu/api/publication/33114978 ID - 33114978 LA - English DB - MTMT ER - TY - JOUR AU - Hudak, Anett AU - Morgan, Gareth AU - Bacovsky, Jaromir AU - Patai, Roland AU - Polgár, Tamás Ferenc AU - Letoha, Annamaria AU - Pettkó-Szandtner, Aladár AU - Vizler, Csaba AU - Szilák, László AU - Letoha, Tamás TI - Biodistribution and Cellular Internalization of Inactivated SARS-CoV-2 in Wild-Type Mice JF - INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES J2 - INT J MOL SCI VL - 23 PY - 2022 IS - 14 PG - 17 SN - 1661-6596 DO - 10.3390/ijms23147609 UR - https://m2.mtmt.hu/api/publication/33050457 ID - 33050457 N1 - Funding Agency and Grant Number: Innovative Medicines Initiative 2 Joint Undertaking [807015]; European Union; EFPIA; European Union [863214]; National Research, Development, and Innovation Office, Hungary [2020-1.1.6-JOVO-2021-00012]; [2017-2.3.6-TET-CN-2018-00023] Funding text: A.H., L.S. and T.L. received funding from the Innovative Medicines Initiative 2 Joint Undertaking under grant agreement no. 807015. This joint undertaking receives support from the European Union's Horizon 2020 research and innovation program and EFPIA. A.H., L.S. and T.L. also received funding from the European Union's Horizon 2020 research and innovation program under Future and Emerging Technologies grant agreement no. 863214. A.H., L.S. and T.L. were also supported by grant no. 2017-2.3.6-TET-CN-2018-00023. A.H., L.S., A.L., P.S.A., C.V. and T.L. were supported by grant no. 2020-1.1.6-JOVO-2021-00012 of the National Research, Development, and Innovation Office, Hungary. AB - Despite the growing list of identified SARS-CoV-2 receptors, the human angiotensin-converting enzyme 2 (ACE2) is still viewed as the main cell entry receptor mediating SARS-CoV-2 internalization. It has been reported that wild-type mice, like other rodent species of the Muridae family, cannot be infected with SARS-CoV-2 due to differences in their ACE2 receptors. On the other hand, the consensus heparin-binding motif of SARS-CoV-2's spike protein, PRRAR, enables the attachment to rodent heparan sulfate proteoglycans (HSPGs), including syndecans, a transmembrane HSPG family with a well-established role in clathrin- and caveolin-independent endocytosis. As mammalian syndecans possess a relatively conserved structure, we analyzed the cellular uptake of inactivated SARS-CoV-2 particles in in vitro and in vivo mice models. Cellular studies revealed efficient uptake into murine cell lines with established syndecan-4 expression. After intravenous administration, inactivated SARS-CoV-2 was taken up by several organs in vivo and could also be detected in the brain. Internalized by various tissues, inactivated SARS-CoV-2 raised tissue TNF-alpha levels, especially in the heart, reflecting the onset of inflammation. Our studies on in vitro and in vivo mice models thus shed light on unknown details of SARS-CoV-2 internalization and help broaden the understanding of the molecular interactions of SARS-CoV-2. LA - English DB - MTMT ER - TY - JOUR AU - Saado, Indira AU - Chia, Khong-Sam AU - Betz, Ruben AU - Alcantara, Andre AU - Pettkó-Szandtner, Aladár AU - Navarrete, Fernando AU - D'Auria, John C. AU - Kolomiets, Michael V AU - Melzer, Michael AU - Feussner, Ivo AU - Djamei, Armin TI - Effector-mediated relocalization of a maize lipoxygenase protein triggers susceptibility to Ustilago maydis JF - PLANT CELL J2 - PLANT CELL VL - 34 PY - 2022 IS - 7 SP - 2785 EP - 2805 PG - 21 SN - 1040-4651 DO - 10.1093/plcell/koac105 UR - https://m2.mtmt.hu/api/publication/32824513 ID - 32824513 N1 - Funding Agency and Grant Number: European Research Council under the European Union's Seventh Framework Program ERC-2013-STG [335691]; Austrian Science Fund (FWF) [I 3033-B22]; Austrian Academy of Sciences (OEAW); Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany's Excellence Strategy [EXC 2070-390732324]; Development and Innovation Office of Hungary [GINOP2.3.2-15-2016-00032] Funding text: The research leading to these results has received funding from the European Research Council under the European Union's Seventh Framework Program ERC-2013-STG, Grant Agreement: 335691, the Austrian Science Fund (FWF): [I 3033-B22], the Austrian Academy of Sciences (OEAW) and the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany's Excellence Strategy (EXC 2070-390732324). A.P.S. was supported by the Development and Innovation Office of Hungary (GINOP2.3.2-15-2016-00032). AB - As the gall-inducing smut fungus Ustilago maydis colonizes maize (Zea mays) plants, it secretes a complex effector blend that suppresses host defense responses, including production of reactive oxygen species (ROS) and redirects host metabolism to facilitate colonization. We show that the U. maydis effector ROS burst interfering protein 1 (Rip1), which is involved in pathogen-associated molecular pattern (PAMP)-triggered suppression of host immunity, is functionally conserved in several other monocot-infecting smut fungi. We also have identified a conserved C-terminal motif essential for Rip1-mediated PAMP-triggered suppression of the ROS burst. The maize susceptibility factor lipoxygenase 3 (Zmlox3) bound by Rip1 was relocalized to the nucleus, leading to partial suppression of the ROS burst. Relocalization was independent of its enzymatic activity, revealing a distinct function for ZmLox3. Most importantly, whereas Zmlox3 maize mutant plants showed increased resistance to U. maydis wild-type strains, rip1 deletion strains infecting the Zmlox3 mutant overcame this effect. This could indicate that Rip1-triggered host resistance depends on ZmLox3 to be suppressed and that lox3 mutation-based resistance of maize to U. maydis requires functional Rip1. Together, our results reveal that Rip1 acts in several cellular compartments to suppress immunity and that targeting of ZmLox3 by Rip1 is responsible for the suppression of Rip1-dependent reduced susceptibility of maize to U. maydis. The fungal effector Rip1, which inhibits pattern-triggered immunity, relocalizes maize lipoxygenase 3 to the plant nucleus, suppressing ROS burst responses in the host that are triggered by pathogen recognition. 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 - Lang, L. AU - Pettkó-Szandtner, Aladár AU - Elbasi, H.T. AU - Takatsuka, H. AU - Nomoto, Y. AU - Zaki, A. AU - Dorokhov, S. AU - De, Jaeger G. AU - Eeckhout, D. AU - Ito, M. AU - Magyar, Zoltán AU - Bögre, L. AU - Heese, M. AU - Schnittger, A. TI - The DREAM complex represses growth in response to DNA damage in Arabidopsis JF - LIFE SCIENCE ALLIANCE J2 - LIFE SCI ALLIANCE VL - 4 PY - 2021 IS - 12 SN - 2575-1077 DO - 10.26508/lsa.202101141 UR - https://m2.mtmt.hu/api/publication/32475639 ID - 32475639 N1 - Funding details: BB/M025047/1 Funding details: GINOP-2.3.2-15-2016-00032 Funding details: 739593 Funding details: NKFIH-K132486 Funding details: Deutsche Forschungsgemeinschaft, DFG, SCHN 736/16-1 Funding details: Japan Society for the Promotion of Science, KAKEN, 18H04833, 20H05408 Funding details: Universität Hamburg, UH Funding text 1: We thank the Single Cell Omics Advanced Core Facility staff of the Hungarian Centre of Excellence for Molecular Medicine (HCEMM) and Biological Research Center for help with their resources and their support. HCEMM has received funding from the EU’s Horizon 2020 research and innovation program (739593). This work was supported through a fellowship of the University of Hamburg to L Lang, a grant by the Development and Innovation Office of Hungary (GINOP-2.3.2-15-2016-00032) to A Pettkó-Szandtner, a grant from the Japan Society for the Promotion of Science KAKENHI (20H05408 and 18H04833) to M Ito, a grant from the Hungarian National Research Funding (NKFIH-K132486) to Z Magyar, a BBSRC-NSF grant (BB/M025047/1) to L Bögre, and a DFG grant (SCHN 736/16-1) to A Schnittger. AB - The DNA of all organisms is constantly damaged by physiological processes and environmental conditions. Upon persistent damage, plant growth and cell proliferation are reduced. Based on previous findings that RBR1, the only Arabidopsis homolog of the mammalian tumor suppressor gene retinoblastoma, plays a key role in the DNA damage response in plants, we unravel here the network of RBR1 interactors under DNA stress conditions. This led to the identification of homologs of every DREAM component in Arabidopsis, including previously not recognized homologs of LIN52. Interestingly, we also discovered NAC044, a mediator of DNA damage response in plants and close homolog of the major DNA damage regulator SOG1, to directly interact with RBR1 and the DREAM component LIN37B. Consistently, not only mutants in NAC044 but also the double mutant of the two LIN37 homologs and mutants for the DREAM component E2FB showed reduced sensitivities to DNA-damaging conditions. Our work indicates the existence of multiple DREAM complexes that work in conjunction with NAC044 to mediate growth arrest after DNA damage. © 2021 Rockefeller University Press. All rights reserved. LA - English DB - MTMT ER -