@article{MTMT:35297282, title = {Mild Heat Stress Alters the Physical State and Structure of Membranes in Triacylglycerol-Deficient Fission Yeast, Schizosaccharomyces pombe}, url = {https://m2.mtmt.hu/api/publication/35297282}, author = {Gudmann, Péter and Gombos, Imre and Péter, Mária and Balogh, Gábor and Török, Zsolt and Vigh, László and Glatz, Attila}, doi = {10.3390/cells13181543}, journal-iso = {CELLS-BASEL}, journal = {CELLS}, volume = {13}, unique-id = {35297282}, abstract = {We investigated whether the elimination of two major enzymes responsible for triacylglycerol synthesis altered the structure and physical state of organelle membranes under mild heat shock conditions in the fission yeast, Schizosaccharomyces pombe. Our study revealed that key intracellular membrane structures, lipid droplets, vacuoles, the mitochondrial network, and the cortical endoplasmic reticulum were all affected in mutant fission yeast cells under mild heat shock but not under normal growth conditions. We also obtained direct evidence that triacylglycerol-deficient cells were less capable than wild-type cells of adjusting their membrane physical properties during thermal stress. The production of thermoprotective molecules, such as HSP16 and trehalose, was reduced in the mutant strain. These findings suggest that an intact system of triacylglycerol metabolism significantly contributes to membrane protection during heat stress.}, year = {2024}, eissn = {2073-4409}, pages = {1543}, orcid-numbers = {Gudmann, Péter/0009-0006-2003-1447; Péter, Mária/0000-0003-0362-6933; Balogh, Gábor/0000-0002-4565-6850; Török, Zsolt/0000-0003-0836-3247; Vigh, László/0000-0001-7450-105X} } @article{MTMT:35177203, title = {Aflatoxin B1 Control by Various Pseudomonas Isolates}, url = {https://m2.mtmt.hu/api/publication/35177203}, author = {Papp, Dóra Anna and Kocsubé, Sándor and Farkas, Zoltán and Szekeres, András and Vágvölgyi, Csaba and Kozma-Bognárné Hamari, Zsuzsanna and Varga, Mónika}, doi = {10.3390/toxins16080367}, journal-iso = {TOXINS}, journal = {TOXINS}, volume = {16}, unique-id = {35177203}, issn = {2072-6651}, year = {2024}, eissn = {2072-6651}, orcid-numbers = {Kocsubé, Sándor/0000-0001-7839-0510; Szekeres, András/0000-0003-1651-4623; Vágvölgyi, Csaba/0000-0003-0009-7773; Kozma-Bognárné Hamari, Zsuzsanna/0000-0001-6374-5083} } @article{MTMT:35176626, title = {Novel method for detecting frequent TERT promoter hot spot mutations in bladder cancer samples.}, url = {https://m2.mtmt.hu/api/publication/35176626}, author = {Kovács, Ákos and Sükösd, Farkas and Kuthi, Levente and Boros, Imre Miklós and Vedelek, Balázs}, doi = {10.1007/s10238-024-01464-3}, journal-iso = {CLIN EXP MED}, journal = {CLINICAL AND EXPERIMENTAL MEDICINE}, volume = {24}, unique-id = {35176626}, issn = {1591-8890}, abstract = {Telomerase reverse transcriptase promoter (TERTp) mutations are frequently targeted tumor markers, however, they reside in regions with high GC content, which poses challenges when examined with simple molecular techniques or even with next-generation sequencing (NGS). In bladder cancer (BC), TERTp mutations are particularly frequent, however, none of the available tools have demonstrated efficacy in detecting TERTp mutations via a simple noninvasive technique. Therefore, we developed a novel PCR-based method for the detection of the two most common TERTp mutations and demonstrated its use for the analysis of BC samples. The developed SHARD-PCR TERTp mutation detection technique requires PCR and restriction digestion steps that are easily implementable even in less well-equipped laboratories. Cell lines with known mutational status were utilized for method development. Matching urine and tumor tissue samples from BC patients were analyzed, and the results were validated by next-generation sequencing. Analysis of eighteen urine and corresponding tumor tissue samples by SHARD-PCR revealed perfect matches in sample pairs, which paralleled the corresponding NGS results: fourteen samples exhibited mutations at the -124 position, two samples showed mutations at the -146 position, and no mutations were detected in two samples. Our study serves as a proof-of-concept and is limited by its small sample size, nonetheless, it demonstrates that SHARD-PCR is a simple, economic and highly reliable method for detecting TERTp mutations, which are common in different cancer types. For bladder cancer, SHARD-PCR can be performed with the use of noninvasive samples and could replace or complement currently used techniques.}, keywords = {bladder cancer; TELOMERASE; telomerase reverse transcriptase; novel method; TERTp mutations}, year = {2024}, eissn = {1591-9528}, pages = {192}, orcid-numbers = {Kuthi, Levente/0000-0001-9247-6679; Boros, Imre Miklós/0000-0001-8504-9687; Vedelek, Balázs/0000-0001-6981-0026} } @article{MTMT:35173369, title = {Mapping of the Lipid-Binding Regions of the Antifungal Protein NFAP2 by Exploiting Model Membranes.}, url = {https://m2.mtmt.hu/api/publication/35173369}, author = {Pavela, Olivér and Juhász, Tünde and Tóth, Liliána and Czajlik, András and Batta, Gyula and Galgóczi, László Norbert and Beke-Somfai, Tamás}, doi = {10.1021/acs.jcim.4c00229}, journal-iso = {J CHEM INF MODEL}, journal = {JOURNAL OF CHEMICAL INFORMATION AND MODELING}, volume = {64}, unique-id = {35173369}, issn = {1549-9596}, abstract = {Fungal infections with high mortality rates represent an increasing health risk. The Neosartorya (Aspergillus) fischeri antifungal protein 2 (NFAP2) is a small, cysteine-rich, cationic protein exhibiting potent anti-Candida activity. As the underlying mechanism, pore formation has been demonstrated; however, molecular level details on its membrane disruption action are lacking. Herein, we addressed the lipid binding of NFAP2 using a combined computational and experimental approach to simple lipid compositions with various surface charge properties. Simulation results revealed binding preferences for negatively charged model membranes, where selectivity is mediated by anionic lipid components enriched at the protein binding site but also assisted by zwitterionic lipid species. Several potential binding routes initiated by various anchoring contacts were observed, which resulted in one main binding mode and a few variants, with NFAP2 residing on the membrane surface. Region 10NCPNNCKHKKG20 of the flexible N-terminal part of the protein showed potency to insert into the lipid bilayer, where the disulfide bond-stabilized short motif 11CPNNC15 could play a key role. In addition, several areas, including the beginning of the N-terminal (residues 1-8), played roles in facilitating initial membrane contacts. Besides, individual roles of residues such as Lys24, Lys32, Lys34, and Trp42 were also revealed by the simulations. Combined data demonstrated that the solution conformation was not perturbed markedly upon membrane interaction, and the folded part of the protein also contributed to stabilizing the bound state. Data also highlighted that the binding of NFAP2 to lipid vesicles is sensitively affected by environmental factors such as ionic strength. Electrostatic interactions driven by anionic lipids were found pivotal, explaining the reduced membrane activity observed under high salt conditions. Experimental data supported the lipid-selective binding mechanisms and pointed to salt-dependent effects, particularly to protein-assisted vesicle aggregation at low ionic strength. Our findings can contribute to the development of NFAP2-based anti-Candida agents and studies aiming at future medical use of peptide-based natural antifungal compounds.}, year = {2024}, eissn = {1549-960X}, pages = {6557-6569}, orcid-numbers = {Tóth, Liliána/0000-0003-1400-6174; Batta, Gyula/0000-0002-0442-1828; Galgóczi, László Norbert/0000-0002-6976-8910} } @article{MTMT:35166799, title = {Chloroplastic ascorbate modifies plant metabolism and may act as a metabolite signal regardless of oxidative stress}, url = {https://m2.mtmt.hu/api/publication/35166799}, author = {Tóth, Dávid and Tengölics, Roland and Aarabi, Fayezeh and Karlsson, Anna and Vidal-Meireles, Andre and Kovács, László and Kuntam, Soujanya and Körmöczi, Tímea and Fernie, Alisdair R and Hudson, Elton P and Papp, Balázs and Tóth, Szilvia Zita}, doi = {10.1093/plphys/kiae409}, journal-iso = {PLANT PHYSIOL}, journal = {PLANT PHYSIOLOGY}, unique-id = {35166799}, issn = {0032-0889}, abstract = {Ascorbate is a major plant metabolite that plays crucial roles in various processes, from reactive oxygen scavenging to epigenetic regulation. However, to what extent and how ascorbate modulates metabolism is largely unknown. We investigated the consequences of chloroplastic and total cellular ascorbate-deficiencies by studying chloroplastic ascorbate-transporter mutant lines lacking PHOSPHATE TRANSPORTER 4; 4 (PHT4; 4) , and the ascorbate-deficient vtc2-4 mutant of Arabidopsis (Arabidopsis thaliana). Under regular growth conditions, both ascorbate deficiencies caused minor alterations in photosynthesis, with no apparent signs of oxidative damage. In contrast, metabolomics analysis revealed global and largely overlapping alterations in the metabolome profiles of both ascorbate-deficiency mutants, suggesting that chloroplastic ascorbate modulates plant metabolism. We observed significant alterations in amino acid metabolism, particularly in arginine metabolism, activation of nucleotide salvage pathways, and changes in secondary metabolism. In addition, proteome-wide analysis of thermostability revealed that ascorbate may interact with enzymes involved in arginine metabolism, the Calvin-Benson cycle, and several photosynthetic electron transport components. Overall, our results suggest that, independently of oxidative stress, chloroplastic ascorbate modulates the activity of diverse metabolic pathways in vascular plants and may act as an internal metabolic signal.}, year = {2024}, eissn = {1532-2548}, orcid-numbers = {Aarabi, Fayezeh/0000-0002-5099-5400; Karlsson, Anna/0009-0003-1867-5698; Körmöczi, Tímea/0000-0002-0973-2473; Fernie, Alisdair R/0000-0001-9000-335X; Hudson, Elton P/0000-0003-1899-7649} } @article{MTMT:35166656, title = {Development of narrow-spectrum topoisomerase-targeting antibacterials against mycobacteria}, url = {https://m2.mtmt.hu/api/publication/35166656}, author = {Sterle, Masa and Habjan, Eva and Piga, Martina and Persolja, Peter and Durcik, Martina and Dernovsek, Jaka and Szili, Petra and Czikkely, Márton Simon and Zidar, Nace and Janez, Ilas and Pál, Csaba and Accetto, Tomaz and Pardo, Luis A. and Kikelj, Danijel and Masic, Lucija Peterlin and Tomasic, Tihomir and Bitter, Wilbert and Cotman, Andrej Emanuel and Speer, Alexander and Zega, Anamarija}, doi = {10.1016/j.ejmech.2024.116693}, journal-iso = {EUR J MED CHEM}, journal = {EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY}, volume = {276}, unique-id = {35166656}, issn = {0223-5234}, abstract = {New 2-pyrrolamidobenzothiazole-based inhibitors of mycobacterial DNA gyrase were discovered. Among these, compounds 49 and 51, show excellent antibacterial activity against Mycobacterium tuberculosis and Mycobacterium abscessus with a notable preference for mycobacteria. Both compounds can penetrate infected macrophages and reduce intracellular M. tuberculosis load. Compound 51 is a potent inhibitor of DNA gyrase (M. tuberculosis DNA gyrase IC50 = 4.1 nM, Escherichia coli DNA gyrase IC50 of <10 nM), selective for bacterial topoisomerases. It displays low MIC90 values (M. tuberculosis: 0.63 M; M. abscessus: 2.5 mu M), showing specificity for mycobacteria, and no apparent toxicity. Compound 49 not only displays potent antimycobacterial activity (MIC90 values of 2.5 mu M for M. tuberculosis and 0.63 mu M for M. abscessus) and selectivity for mycobacteria but also exhibits favorable solubility (kinetic solubility = 55 mu M) and plasma protein binding (with a fraction unbound of 2.9 % for human and 4.7 % for mouse). These findings underscore the potential of fine-tuning molecular properties to develop DNA gyrase B inhibitors that specifically target the mycobacterial chemical space, mitigating the risk of resistance development in non-target pathogens and minimizing harm to the microbiome.}, keywords = {DNA GYRASE; DNA GYRASE; tuberculosis; DRUG-RESISTANCE; Mycobacterium tuberculosis; benzothiazole; nontuberculous mycobacteria; Mycobacterium abscessus}, year = {2024}, eissn = {1768-3254} } @misc{MTMT:35152251, title = {Unraveling Morphogenesis, Starvation, and Light Responses in a Mushroom-Forming Fungus, Coprinopsis cinerea, Using Long Read Sequencing and Extensive Expression Profiling}, url = {https://m2.mtmt.hu/api/publication/35152251}, author = {Botond, Hegedüs and Neha, Sahu and Balázs, Bálint and Sajeet, Haridas and Viktória, Bense and Zsolt, Merényi and Máté, Virágh and Hongli, Wu and Xiao-Bin, Liu and Robert, Riley and Anna, Lipzen and Maxim, Koriabine and Emily, Savage and Jie, Guo and Kerrie, Barry and Vivian, Ng and Péter, Urbán and Attila, Gyenesei and Michael, Freitag and Igor, V. Grigoriev and Nagy, László}, doi = {10.1101/2024.05.10.593147}, unique-id = {35152251}, year = {2024} } @misc{MTMT:35152218, title = {A new regulator of sporulation sheds light on spore morphogenesis and ballistospory in mushroom-forming fungi}, url = {https://m2.mtmt.hu/api/publication/35152218}, author = {Zhihao, Hou and Zsolt, Merényi and Yashu, Yang and Yan, Zhang and Árpád, Csernetics and Balázs, Bálint and Botond, Hegedüs and Csenge, Földi and Hongli, Wu and Zsolt, Kristóffy and Edit, Ábrahám and Nikolett, Miklovics and Máté, Virágh and Xiao-Bin, Liu and Nikolett, Zsibrita and Zoltán, Lipinszki and Ildiko, Karcagi and Wei, Gao and Nagy, László}, doi = {10.1101/2024.07.26.604922}, unique-id = {35152218}, year = {2024} } @article{MTMT:35149771, title = {Phylogenomics, divergence times and notes of orders in Basidiomycota}, url = {https://m2.mtmt.hu/api/publication/35149771}, author = {He, M.-Q. and Cao, B. and Liu, F. and Boekhout, T. and Denchev, T.T. and Schoutteten, N. and Denchev, C.M. and Kemler, M. and Gorjón, S.P. and Begerow, D. and Valenzuela, R. and Davoodian, N. and Niskanen, T. and Vizzini, A. and Redhead, S.A. and Ramírez-Cruz, V. and Papp, Viktor and Dudka, V.A. and Dutta, A.K. and García-Sandoval, R. and Liu, X.-Z. and Kijpornyongpan, T. and Savchenko, A. and Tedersoo, L. and Theelen, B. and Trierveiler-Pereira, L. and Wu, F. and Zamora, J.C. and Zeng, X.-Y. and Zhou, L.-W. and Liu, S.-L. and Ghobad-Nejhad, M. and Giachini, A.J. and Li, G.-J. and Kakishima, M. and Olariaga, I. and Haelewaters, D. and Sulistyo, B. and Sugiyama, J. and Svantesson, S. and Yurkov, A. and Alvarado, P. and Antonín, V. and da, Silva A.F. and Druzhinina, I. and Gibertoni, T.B. and Guzmán-Dávalos, L. and Justo, A. and Karunarathna, S.C. and Galappaththi, M.C.A. and Toome-Heller, M. and Hosoya, T. and Liimatainen, K. and Márquez, R. and Mešić, A. and Moncalvo, J.-M. and Nagy, László and Varga, Torda and Orihara, T. and Raymundo, T. and Salcedo, I. and Silva-Filho, A.G.S. and Tkalčec, Z. and Wartchow, F. and Zhao, C.-L. and Bau, T. and Cabarroi-Hernández, M. and Cortés-Pérez, A. and Decock, C. and De, Lange R. and Weiss, M. and Menolli, N. Jr. and Nilsson, R.H. and Fan, Y.-G. and Verbeken, A. and Gafforov, Y. and Meiras-Ottoni, A. and Mendes-Alvarenga, R.L. and Zeng, N.-K. and Wu, Q. and Hyde, K.D. and Kirk, P.M. and Zhao, R.-L.}, doi = {10.1007/s13225-024-00535-w}, journal-iso = {FUNGAL DIVERS}, journal = {FUNGAL DIVERSITY}, volume = {126}, unique-id = {35149771}, issn = {1560-2745}, abstract = {Basidiomycota is one of the major phyla in the fungal tree of life. The outline of Basidiomycota provides essential taxonomic information for researchers and workers in mycology. In this study, we present a time-framed phylogenomic tree with 487 species of Basidiomycota from 127 families, 47 orders, 14 classes and four subphyla; we update the outline of Basidiomycota based on the phylogenomic relationships and the taxonomic studies since 2019; and we provide notes for each order and discuss the history, defining characteristics, evolution, justification of orders, problems, significance, and plates. Our phylogenomic analysis suggests that the subphyla diverged in a time range of 443–490 Myr (million years), classes in a time range of 312–412 Myr, and orders in a time range of 102–361 Myr. Families diverged in a time range of 50–289 Myr, 76–224 Myr, and 62–156 Myr in Agaricomycotina, Pucciniomycotina, and Ustilaginomycotina, respectively. Based on the phylogenomic relationships and divergence times, we propose a new suborder Mycenineae in Agaricales to accommodate Mycenaceae. In the current outline of Basidiomycota, there are four subphyla, 20 classes, 77 orders, 297 families, and 2134 genera accepted. When building a robust taxonomy of Basidiomycota in the genomic era, the generation of molecular phylogenetic data has become relatively easier. Finding phenotypical characters, especially those that can be applied for identification and classification, however, has become increasingly challenging. © The Author(s) under exclusive licence to Mushroom Research Foundation 2024.}, keywords = {CLASSIFICATION; taxonomy; Fungi; SYSTEMATICS; molecular clock}, year = {2024}, eissn = {1878-9129}, pages = {127-406}, orcid-numbers = {Varga, Torda/0000-0002-2597-9126} } @article{MTMT:35135174, title = {Dominant suppressor genes of p53-induced apoptosis in Drosophila melanogaster}, url = {https://m2.mtmt.hu/api/publication/35135174}, author = {Szlanka, Tamás and Lukacsovich, Tamás and Bálint, Éva and Virágh, Eszter Erika and Szabó, Kornélia and Hajdú, Ildikó and Molnár, Enikő and Lin, Yu-Hsien and Zvara, Ágnes and Kelemen-Valkony, Ildikó and Méhi, Orsolya Katinka and Török, István and Hegedűs, Zoltán and Kiss, Brigitta and Ramasz, Beáta and Magdalena, Laura M and Puskás, László and Mechler, Bernard M and Fónagy, Adrien and Asztalos, Zoltán Imre and Steinbach, Gábor and Žurovec, Michal and Boros, Imre Miklós and Kiss, István}, doi = {10.1093/g3journal/jkae149}, journal-iso = {G3-GENES GENOM GENET}, journal = {G3-GENES GENOMES GENETICS}, volume = {14}, unique-id = {35135174}, issn = {2160-1836}, abstract = {One of a major function of programmed cell death (apoptosis) is the removal of cells which suffered oncogenic mutations, thereby preventing cancerous transformation. By making use of a Double-Headed-EP (DEP) transposon, a P element derivative made in our laboratory, we made an insertional mutagenesis screen in Drosophila melanogaster to identify genes which, when overexpressed, suppress the p53-activated apoptosis. The DEP element has Gal4-activatable, outward-directed UAS-promoters at both ends which can be deleted separately in vivo. In the DEP insertion mutants, we used the GMR-Gal4 driver to induce transcription from both UAS-promoters and tested the suppression effect on the apoptotic rough eye phenotype generated by an activated UAS-p53 transgene. By DEP insertions, seven genes were identified which suppressed the p53-induced apoptosis. In four mutants, the suppression effect resulted from single genes activated by one UAS-promoter (Pka-R2, Rga, crol, Spt5). In the other three (Orct2, Polr2M, stg), deleting either UAS-promoter eliminated the suppression effect. In qPCR experiments we found that the genes in the vicinity of the DEP insertion also showed an elevated expression level. This suggested an additive effect of the nearby genes on suppressing apoptosis. In the eucaryotic genomes there are co-expressed gene clusters. Three of the DEP insertion mutants are included and two are in close vicinity of separate co-expressed gene clusters. This raises the possibility that the activity of some of the genes in these clusters may help the suppression of the apoptotic cell death.}, keywords = {APOPTOSIS; DROSOPHILA; SUPPRESSION; p53; activating insertional mutagenesis}, year = {2024}, eissn = {2160-1836}, orcid-numbers = {Méhi, Orsolya Katinka/0009-0004-7918-913X; Steinbach, Gábor/0000-0001-7137-7030; Boros, Imre Miklós/0000-0001-8504-9687} }