TY - THES AU - Hegedűs, Lili TI - A PARI fehérje szerepe a rekombináció-függő folyamatok szabályozásában elakadt replikációs villa esetén [The role of the PARI protein in the regulation of recombination-dependent mechanisms at the stalled replication fork] PB - Szegedi Tudományegyetem (SZTE) PY - 2022 SP - 74 DO - 10.14232/phd.11049 UR - https://m2.mtmt.hu/api/publication/33095648 ID - 33095648 AB - Egy DNS-hiba következtében elakadt replikációs villa menekítése többféleképpen is megvalósulhat a sejtekben. Az, hogy melyik útvonal aktív, szigorú szabályozás alatt áll, hiszen nem mindegy, hogy a sejtekben egy gyors, ám mutagén transzléziós szintézis zajlik vagy éppen egy bonyolult struktúrákon végbemenő, de pontos másolást lehetővé tevő templátváltás. Ezen mechanizmusok közötti molekuláris kapcsoló a PCNA fehérje, illetve annak poszttranszlációs módosításai. Míg ubiquitilációja a DNS-hibatolerancia útvonalakat aktiválja, addig SUMOilációja a rekombináció-függő folyamatot gátolja. Utóbbiban élesztőben végzett vizsgálatok alapján fontos szerepet tölt be az Srs2 fehérje, több szinten hatva. Helikáz aktivitása révén részt vesz a D-hurok szétszerelésében, SUMOilált PCNA-függő módon pedig a D-hurok meghosszabbítását gátolja. Humán sejtekben ezeket a funkciókat több fehérje látja el, melyek közül a PARI-ról mutatták ki, hogy kölcsönhatásba lép a SUMOilált PCNA-vel. Munkánk során azt vizsgáltuk, hogy a PARI fehérje milyen molekuláris mechanizmusok révén valósítja meg a homológ rekombináció gátlását az elakadt replikációs villa menekítésekor: a D-hurok meghosszabbításának gátlása során megakadályozza, hogy a homológ szakaszról hosszasan történjen meg a duplikáció, lecsökkentve az esélyét az átkereszteződéseknek és meggátolva a további rekombinációs eseményeket és az esetleges genomi átrendeződéseket. LA - Hungarian DB - MTMT ER - TY - JOUR AU - Fenteany, Gabriel AU - Gaur, Paras AU - Hegedűs, Lili AU - Dudás, Kata AU - Kiss, Ernő AU - Wéber, Edit AU - Hackler, László AU - Martinek, Tamás AU - Puskás, László AU - Haracska, Lajos TI - Multilevel structure–activity profiling reveals multiple green tea compound families that each modulate ubiquitin-activating enzyme and ubiquitination by a distinct mechanism JF - SCIENTIFIC REPORTS J2 - SCI REP VL - 9 PY - 2019 IS - 1 PG - 16 SN - 2045-2322 DO - 10.1038/s41598-019-48888-6 UR - https://m2.mtmt.hu/api/publication/30791081 ID - 30791081 N1 - Funding Agency and Grant Number: National Research, Development and Innovation Office [GINOP-2.3.2-15-2016-00020, GINOP-2.3.2-15-2016-00026]; European Union [739593] Funding text: We wish to thank Katalin Kovacs, Gaurav Sharma, Lajos Pinter, and Monika Morocz for technical assistance. This work was supported by the National Research, Development and Innovation Office (GINOP-2.3.2-15-2016-00020 and GINOP-2.3.2-15-2016-00026). This project has also received funding from the European Union's Horizon 2020 research and innovation programme under grant agreement No. 739593. HCEMM-BRC Mutagenesis and Carcinogenesis Research Group, Institute of Genetics, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, 6726, Hungary Department of Medical Chemistry, University of Szeged, Szeged, 6720, Hungary AstridBio Technologies Ltd., Szeged, 6726, Hungary Laboratory of Functional Genomics, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, 6726, Hungary Avicor Ltd., Szeged, 6726, Hungary Cited By :2 Export Date: 11 May 2021 Correspondence Address: Fenteany, G.; HCEMM-BRC Mutagenesis and Carcinogenesis Research Group, Hungary; email: fenteany.gabriel@brc.mta.hu Funding Agency and Grant Number: National Research, Development and Innovation OfficeNational Research, Development & Innovation Office (NRDIO) - Hungary [GINOP-2.3.2-15-2016-00020, GINOP-2.3.2-15-2016-00026]; European UnionEuropean Commission [739593] Funding text: We wish to thank Katalin Kovacs, Gaurav Sharma, Lajos Pinter, and Monika Morocz for technical assistance. This work was supported by the National Research, Development and Innovation Office (GINOP-2.3.2-15-2016-00020 and GINOP-2.3.2-15-2016-00026). This project has also received funding from the European Union's Horizon 2020 research and innovation programme under grant agreement No. 739593. LA - English DB - MTMT ER - TY - JOUR AU - Peng, M AU - Cong, K AU - Panzarino, NJ AU - Nayak, S AU - Calvo, J AU - Deng, B AU - Zhu, LJ AU - Mórocz, Mónika AU - Hegedűs, Lili AU - Haracska, Lajos AU - Cantor, SB TI - Opposing Roles of FANCJ and HLTF Protect Forks and Restrain Replication during Stress JF - CELL REPORTS J2 - CELL REP VL - 24 PY - 2018 IS - 12 SP - 3251 EP - 3261 PG - 11 SN - 2211-1247 DO - 10.1016/j.celrep.2018.08.065 UR - https://m2.mtmt.hu/api/publication/27695954 ID - 27695954 N1 - Funding Agency and Grant Number: NIH [R01 CA176166-01A1]; Lipp Family Foundation; NIH from the INBRE Program of the National Institute of General Medical Science [P20GM103449]; National Research, Development and Innovation Office [GINOP-2.3.2-15-2016-00026, GINOP-2.3.2-15-2016-00024] Funding text: We thank the members of the Cantor laboratory for helpful discussions and Jianhong Ou for help with data analysis. This work was supported by NIH grant R01 CA176166-01A1, as well as charitable contributions from Mr. and Mrs. Edward T. Vitone, Jr. and the Lipp Family Foundation. The Vermont Genetics Network Proteomics Facility is supported through NIH grant P20GM103449 from the INBRE Program of the National Institute of General Medical Science. The Lajos laboratory is supported by the National Research, Development and Innovation Office (grants GINOP-2.3.2-15-2016-00026 and GINOP-2.3.2-15-2016-00024). AB - The DNA helicase FANCJ is mutated in hereditary breast and ovarian cancer and Fanconi anemia (FA). Nevertheless, how loss of FANCJ translates to disease pathogenesis remains unclear. We addressed this question by analyzing proteins associated with replication forks in cells with or without FANCJ. We demonstrate that FANCJ-knockout (FANCJ-KO) cells have alterations in the replisome that are consistent with enhanced replication stress, including an aberrant accumulation of the fork remodeling factor helicase-like transcription factor (HLTF). Correspondingly, HLTF contributes to fork degradation in FANCJ-KO cells. Unexpectedly, the unrestrained DNA synthesis that characterizes HLTF-deficient cells is FANCJ dependent and correlates with S1 nuclease sensitivity and fork degradation. These results suggest that FANCJ and HLTF promote replication fork integrity, in part by counteracting each other to keep fork remodeling and elongation in check. Indicating one protein compensates for loss of the other, loss of both HLTF and FANCJ causes a more severe replication stress response. LA - English DB - MTMT ER - TY - JOUR AU - Braskó, Csilla AU - Smith, K AU - Molnár, Csaba AU - Faragó, Nóra AU - Hegedűs, Lili AU - Bálind, Árpád AU - Balassa, Tamás AU - Szkalisity, Ábel AU - Sükösd, Farkas AU - Kocsis, Ágnes Katalin AU - Bálint, Balázs AU - Paavolainen, L AU - Enyedi, Márton Zsolt AU - Nagy, István AU - Puskás, László AU - Haracska, Lajos AU - Tamás, Gábor AU - Horváth, Péter TI - Intelligent image-based in situ single-cell isolation JF - NATURE COMMUNICATIONS J2 - NAT COMMUN VL - 9 PY - 2018 IS - 1 PG - 7 SN - 2041-1723 DO - 10.1038/s41467-017-02628-4 UR - https://m2.mtmt.hu/api/publication/3318793 ID - 3318793 N1 - University of Szeged, Hungary Közép fasor 52, Szeged, 6726, Hungary School of Computer Science and Communication, KTH Royal Institute of Technology, Lindstedtsvägen 3-5, Stockholm, 10044, Sweden Science for Life Laboratory, Tomtebodavägen 23A, Solna, 17121, Sweden Biological Research Centre, Hungarian Academy of Sciences, Temesvári krt. 62., Szeged, 6726, Hungary Avidin Biotechnology Ltd, Alsó Kiköto sor 11, Szeged, 6726, Hungary SeqOmics Biotechnology Ltd, Vállalkozók útja 7, Mórahalom, 6782, Hungary Institute for Molecular Medicine Finland (FIMM), University of Helsinki, Tukholmankatu 8, Helsinki, 00014, Finland Cited By :17 Export Date: 26 August 2019 Correspondence Address: Horvath, P.; Biological Research Centre, Hungarian Academy of Sciences, Temesvári krt. 62., Hungary; email: horvath.peter@brc.mta.hu Funding details: VKSZ-14-1-2015-0155 Funding details: Magyar Tudományos Akadémia, MTA Funding details: Tekes, 40294/13 Funding text 1: A.B., C.B., T.B. and P.H. acknowledge the Hungarian National Brain Research Program (MTA-SE-NAP B-BIOMAG). P.H. and L.P. acknowledge support from the Finnish TEKES FiDiPro Fellow Grant 40294/13. N.F. and G.T. were supported by the National Research, Development and Innovation Office of Hungary (VKSZ-14-1-2015-0155), the Hungarian Academy of Sciences and the ERC INTERIMPACT project. P.H. and I.N. were supported by the János Bolyai Research Scholarship of the Hungarian Academy of Sciences. L.H. and P.H. acknowledge the European Union and the European Regional Development Funds (GINOP-2.3.2-15-2016-00006, GINOP-2.3.2-15-2016-00020). University of Szeged, Hungary Közép fasor 52, Szeged, 6726, Hungary School of Computer Science and Communication, KTH Royal Institute of Technology, Lindstedtsvägen 3-5, Stockholm, 10044, Sweden Science for Life Laboratory, Tomtebodavägen 23A, Solna, 17121, Sweden Biological Research Centre, Hungarian Academy of Sciences, Temesvári krt. 62., Szeged, 6726, Hungary Avidin Biotechnology Ltd, Alsó Kiköto sor 11, Szeged, 6726, Hungary SeqOmics Biotechnology Ltd, Vállalkozók útja 7, Mórahalom, 6782, Hungary Institute for Molecular Medicine Finland (FIMM), University of Helsinki, Tukholmankatu 8, Helsinki, 00014, Finland Cited By :19 Export Date: 28 January 2020 Correspondence Address: Horvath, P.; Biological Research Centre, Hungarian Academy of Sciences, Temesvári krt. 62., Hungary; email: horvath.peter@brc.mta.hu Funding details: VKSZ-14-1-2015-0155 Funding details: Magyar Tudományos Akadémia, MTA Funding details: Tekes, 40294/13 Funding text 1: A.B., C.B., T.B. and P.H. acknowledge the Hungarian National Brain Research Program (MTA-SE-NAP B-BIOMAG). P.H. and L.P. acknowledge support from the Finnish TEKES FiDiPro Fellow Grant 40294/13. N.F. and G.T. were supported by the National Research, Development and Innovation Office of Hungary (VKSZ-14-1-2015-0155), the Hungarian Academy of Sciences and the ERC INTERIMPACT project. P.H. and I.N. were supported by the János Bolyai Research Scholarship of the Hungarian Academy of Sciences. L.H. and P.H. acknowledge the European Union and the European Regional Development Funds (GINOP-2.3.2-15-2016-00006, GINOP-2.3.2-15-2016-00020). Funding Agency and Grant Number: Hungarian National Brain Research Program (MTA-SE-NAP B-BIOMAG); Finnish TEKES FiDiPro [40294/13]; National Research, Development and Innovation Office of Hungary [VKSZ-14-1-2015-0155]; Hungarian Academy of SciencesHungarian Academy of Sciences; ERC INTERIMPACT; European UnionEuropean Union (EU); European Regional Development FundsEuropean Union (EU) [GINOP-2.3.2-15-2016-00006, GINOP-2.3.2-15-2016-00020] Funding text: A.B., C.B., T.B. and P.H. acknowledge the Hungarian National Brain Research Program (MTA-SE-NAP B-BIOMAG). P.H. and L.P. acknowledge support from the Finnish TEKES FiDiPro Fellow Grant 40294/13. N.F. and G.T. were supported by the National Research, Development and Innovation Office of Hungary (VKSZ-14-1-2015-0155), the Hungarian Academy of Sciences and the ERC INTERIMPACT project. P.H. and I.N. were supported by the Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences. L.H. and P. H. acknowledge the European Union and the European Regional Development Funds (GINOP-2.3.2-15-2016-00006, GINOP-2.3.2-15-2016-00020). University of Szeged, Hungary Közép fasor 52, Szeged, 6726, Hungary School of Computer Science and Communication, KTH Royal Institute of Technology, Lindstedtsvägen 3-5, Stockholm, 10044, Sweden Science for Life Laboratory, Tomtebodavägen 23A, Solna, 17121, Sweden Biological Research Centre, Hungarian Academy of Sciences, Temesvári krt. 62., Szeged, 6726, Hungary Avidin Biotechnology Ltd, Alsó Kiköto sor 11, Szeged, 6726, Hungary SeqOmics Biotechnology Ltd, Vállalkozók útja 7, Mórahalom, 6782, Hungary Institute for Molecular Medicine Finland (FIMM), University of Helsinki, Tukholmankatu 8, Helsinki, 00014, Finland Cited By :26 Export Date: 28 August 2020 Correspondence Address: Horvath, P.; Biological Research Centre, Hungarian Academy of Sciences, Temesvári krt. 62., Hungary; email: horvath.peter@brc.mta.hu Funding details: VKSZ-14-1-2015-0155 Funding details: Magyar Tudományos Akadémia, MTA Funding details: European Commission, EC Funding details: European Research Council, ERC Funding details: GINOP-2.3.2-15-2016-00006, GINOP-2.3.2-15-2016-00020 Funding details: 40294/13 Funding text 1: A.B., C.B., T.B. and P.H. acknowledge the Hungarian National Brain Research Program (MTA-SE-NAP B-BIOMAG). P.H. and L.P. acknowledge support from the Finnish TEKES FiDiPro Fellow Grant 40294/13. N.F. and G.T. were supported by the National Research, Development and Innovation Office of Hungary (VKSZ-14-1-2015-0155), the Hungarian Academy of Sciences and the ERC INTERIMPACT project. P.H. and I.N. were supported by the János Bolyai Research Scholarship of the Hungarian Academy of Sciences. L.H. and P.H. acknowledge the European Union and the European Regional Development Funds (GINOP-2.3.2-15-2016-00006, GINOP-2.3.2-15-2016-00020). AB - Quantifying heterogeneities within cell populations is important for many fields including cancer research and neurobiology; however, techniques to isolate individual cells are limited. Here, we describe a high-throughput, non-disruptive, and cost-effective isolation method that is capable of capturing individually targeted cells using widely available techniques. Using high-resolution microscopy, laser microcapture microscopy, image analysis, and machine learning, our technology enables scalable molecular genetic analysis of single cells, targetable by morphology or location within the sample. LA - English DB - MTMT ER - TY - JOUR AU - Tóth, Ágnes AU - Hegedűs, Lili AU - Juhász, Szilvia AU - Haracska, Lajos AU - Burkovics, Péter TI - The DNA-binding box of human SPARTAN contributes to the targeting of Poleta to DNA damage sites. JF - DNA REPAIR J2 - DNA REPAIR VL - 49 PY - 2017 SP - 33 EP - 42 PG - 10 SN - 1568-7864 DO - 10.1016/j.dnarep.2016.10.007 UR - https://m2.mtmt.hu/api/publication/3140736 ID - 3140736 AB - Inappropriate repair of UV-induced DNA damage results in human diseases such as Xeroderma pigmentosum (XP), which is associated with an extremely high risk of skin cancer. A variant form of XP is caused by the absence of Poleta, which is normally able to bypass UV-induced DNA lesions in an error-free manner. However, Poleta is highly error prone when replicating undamaged DNA and, thus, the regulation of the proper targeting of Poleta is crucial for the prevention of mutagenesis and UV-induced cancer formation. Spartan is a novel regulator of the damage tolerance pathway, and its association with Ub-PCNA has a role in Poleta targeting; however, our knowledge about its function is only rudimentary. Here, we describe a new biochemical property of purified human SPARTAN by showing that it is a DNA-binding protein. Using a DNA binding mutant, we provide in vivo evidence that DNA binding by SPARTAN regulates the targeting of Poleta to damage sites after UV exposure, and this function contributes highly to its DNA-damage tolerance function. LA - English DB - MTMT ER - TY - GEN AU - Hegedűs, Lili TI - A PARI fehérje, mint a homológ rekombináció szuppresszora PY - 2016 UR - https://m2.mtmt.hu/api/publication/3083577 ID - 3083577 LA - Hungarian DB - MTMT ER - TY - GEN AU - Dudas, K AU - Hegedűs, Lili AU - Haracska, L AU - Burkovics, P TI - Regulation of DNA damage tolerance by ZBTB1 PY - 2016 UR - https://m2.mtmt.hu/api/publication/3083377 ID - 3083377 LA - English DB - MTMT ER - TY - CHAP AU - Hegedűs, Lili AU - Sebesta, M AU - Altmannova, V AU - Haracska, L AU - Krejci, L AU - Burkovics, P ED - Chovanec, Miroslav TI - PARI as a regulator of homologous recombination T2 - 7th DNA Repair Workshop PB - Cancer Research Institute, Slovak Academy of Sciences CY - Bratislava SN - 9788026310426 PY - 2016 UR - https://m2.mtmt.hu/api/publication/3083365 ID - 3083365 LA - English DB - MTMT ER - TY - CONF AU - Dudas, K AU - Hegedűs, Lili AU - Haracska, L AU - Burkovics, P ED - Páy, Anikó TI - Regulation of DNA damage tolerance by ZBTB1 T2 - Straub-napok PY - 2016 UR - https://m2.mtmt.hu/api/publication/3082928 ID - 3082928 LA - English DB - MTMT ER - TY - CONF AU - Zsigmond, Eszter AU - Morocz, M AU - Toth, R AU - Berczeli, Orsolya AU - Hegedűs, Lili AU - Juhasz, S AU - Haracska, L ED - Páy, Anikó TI - The role of human Spartan in the maintenance of genome integrity T2 - Straub-napok PY - 2016 UR - https://m2.mtmt.hu/api/publication/3082794 ID - 3082794 LA - Hungarian DB - MTMT ER -