TY - JOUR AU - Sidorov, R AU - Kucerova, L AU - Kiss, István AU - Zurovec, M TI - Mutation in the Drosophila melanogaster adenosine receptor gene selectively decreases the mosaic hyperplastic epithelial outgrowth rates in wts or dco heterozygous flies JF - PURINERGIC SIGNALLING J2 - PURINERG SIGNAL VL - 11 PY - 2015 IS - 1 SP - 95 EP - 105 PG - 11 SN - 1573-9538 DO - 10.1007/s11302-014-9435-2 UR - https://m2.mtmt.hu/api/publication/2879395 ID - 2879395 AB - Adenosine (Ado) is a ubiquitous metabolite that plays a prominent role as a paracrine homeostatic signal of metabolic imbalance within tissues. It quickly responds to various stress stimuli by adjusting energy metabolism and influencing cell growth and survival. Ado is also released by dead or dying cells and is present at significant concentrations in solid tumors. Ado signaling is mediated by Ado receptors (AdoR) and proteins modulating its concentration, including nucleoside transporters and Ado deaminases. We examined the impact of genetic manipulations of three Drosophila genes involved in Ado signaling on the incidence of somatic mosaic clones formed by the loss of heterozygosity (LOH) of tumor suppressor and marker genes. We show here that genetic manipulations with the AdoR, equilibrative nucleoside transporter 2 (Ent2), and Ado deaminase growth factor-A (Adgf-A) cause dramatic changes in the frequency of hyperplastic outgrowth clones formed by LOH of the warts (wts) tumor suppressor, while they have almost no effect on control yellow (y) clones. In addition, the effect of AdoR is dose-sensitive and its overexpression leads to the increase in wts hyperplastic epithelial outgrowth rates. Consistently, the frequency of mosaic hyperplastic outgrowth clones generated by the LOH of another tumor suppressor, discs overgrown (dco), belonging to the wts signaling pathway is also dependent on AdoR. Our results provide interesting insight into the maintenance of tissue homeostasis at a cellular level. LA - English DB - MTMT ER - TY - JOUR AU - Benbahouche, NE AU - Iliopoulos, I AU - Torok, I AU - Marhold, J AU - Henri, J AU - Kajava, AV AU - Farkas, R AU - Kempf, T AU - Schnolzer, M AU - Meyer, P AU - Kiss, István AU - Bertrand, E AU - Mechler, BM AU - Pradet-Balade, B TI - Drosophila Spag Is the Homolog of RNA Polymerase II-associated Protein 3 (RPAP3) and Recruits the Heat Shock Proteins 70 and 90 (Hsp70 and Hsp90) during the Assembly of Cellular Machineries JF - JOURNAL OF BIOLOGICAL CHEMISTRY J2 - J BIOL CHEM VL - 289 PY - 2014 IS - 9 SP - 6236 EP - 6247 PG - 12 SN - 0021-9258 DO - 10.1074/jbc.M113.499608 UR - https://m2.mtmt.hu/api/publication/2839637 ID - 2839637 AB - Background: Mammalian RNA polymerase II-associated protein 3 (RPAP3) recruits heat shock protein 90 (Hsp90) to assemble cellular machineries such as RNA polymerases. Results:Spaghetti encodes the Drosophila homolog of RPAP3. Spaghetti is essential for development. Spag protein binds and stimulates Hsp90 and Hsp70. Conclusion: RPAP3 function is conserved among metazoans. Significance: Our data suggest that Hsp70 assists RPAP3 in complex assembly. The R2TP is a recently identified Hsp90 co-chaperone, composed of four proteins as follows: Pih1D1, RPAP3, and the AAA(+)-ATPases RUVBL1 and RUVBL2. In mammals, the R2TP is involved in the biogenesis of cellular machineries such as RNA polymerases, small nucleolar ribonucleoparticles and phosphatidylinositol 3-kinase-related kinases. Here, we characterize the spaghetti (spag) gene of Drosophila, the homolog of human RPAP3. This gene plays an essential function during Drosophila development. We show that Spag protein binds Drosophila orthologs of R2TP components and Hsp90, like its yeast counterpart. Unexpectedly, Spag also interacts and stimulates the chaperone activity of Hsp70. Using null mutants and flies with inducible RNAi, we show that spaghetti is necessary for the stabilization of snoRNP core proteins and target of rapamycin activity and likely the assembly of RNA polymerase II. This work highlights the strong conservation of both the HSP90/R2TP system and its clients and further shows that Spag, unlike Saccharomyces cerevisiae Tah1, performs essential functions in metazoans. Interaction of Spag with both Hsp70 and Hsp90 suggests a model whereby R2TP would accompany clients from Hsp70 to Hsp90 to facilitate their assembly into macromolecular complexes. LA - English DB - MTMT ER - TY - JOUR AU - Kiss, Brigitta AU - Szlanka, Tamás AU - Zvara, Ágnes AU - Michal, Žurovec AU - Michal, Sery AU - Štefan, Kakaš AU - Ramasz, Beáta AU - Hegedűs, Zoltán AU - Tamás, Lukacsovich AU - Puskás, László AU - Fónagy, Adrien AU - Kiss, István TI - Selective elimination/RNAi silencing of FMRF-related peptides and their receptors decreases the locomotor activity in Drosophila melanogaster JF - GENERAL AND COMPARATIVE ENDOCRINOLOGY J2 - GEN COMP ENDOCR VL - 191 PY - 2013 SP - 137 EP - 145 PG - 9 SN - 0016-6480 DO - 10.1016/j.ygcen.2013.05.023 UR - https://m2.mtmt.hu/api/publication/2383668 ID - 2383668 LA - English DB - MTMT ER - TY - JOUR AU - Muha, Villő AU - Horváth, András AU - Békési, Angéla AU - Pukáncsik, Mária AU - Hodoscsek, B AU - Merényi, Gábor AU - Róna, Gergely AU - Batki, J AU - Kiss, István AU - Jankovics, Ferenc AU - Vilmos, Péter AU - Erdélyi, Miklós AU - Vértessy, Beáta (Grolmuszné) TI - Uracil-Containing DNA in Drosophila: Stability, Stage-Specific Accumulation, and Developmental Involvement JF - PLOS GENETICS J2 - PLOS GENET VL - 8 PY - 2012 IS - 6 PG - 9 SN - 1553-7390 DO - 10.1371/journal.pgen.1002738 UR - https://m2.mtmt.hu/api/publication/2034630 ID - 2034630 N1 - Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Science, Budapest, Hungary Institute of Genetics, Biological Research Centre (BRC), Hungarian Academy of Science, Szeged, Hungary Department of Applied Biotechnology and Food Sciences, University of Technology and Economics, Budapest, Hungary Cited By :49 Export Date: 6 May 2021 Correspondence Address: Vértessy, B. G.; Institute of Enzymology, , Budapest, Hungary; email: vertessy@enzim.hu Chemicals/CAS: DNA, 9007-49-2; deoxyuridine triphosphate pyrophosphatase, 37289-34-2; uracil, 66-22-8; inorganic pyrophosphatase, 9024-82-2, 9033-44-7; uracil DNA glycosidase, 59088-21-0; DNA, 9007-49-2; Pyrophosphatases, 3.6.1.-; Uracil, 66-22-8; Uracil-DNA Glycosidase, 3.2.2.-; dUTP pyrophosphatase, 3.6.1.23 Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Science, Budapest, Hungary Institute of Genetics, Biological Research Centre (BRC), Hungarian Academy of Science, Szeged, Hungary Department of Applied Biotechnology and Food Sciences, University of Technology and Economics, Budapest, Hungary Cited By :49 Export Date: 7 May 2021 Correspondence Address: Vértessy, B. G.; Institute of Enzymology, , Budapest, Hungary; email: vertessy@enzim.hu Chemicals/CAS: DNA, 9007-49-2; deoxyuridine triphosphate pyrophosphatase, 37289-34-2; uracil, 66-22-8; inorganic pyrophosphatase, 9024-82-2, 9033-44-7; uracil DNA glycosidase, 59088-21-0; DNA, 9007-49-2; Pyrophosphatases, 3.6.1.-; Uracil, 66-22-8; Uracil-DNA Glycosidase, 3.2.2.-; dUTP pyrophosphatase, 3.6.1.23 Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Science, Budapest, Hungary Institute of Genetics, Biological Research Centre (BRC), Hungarian Academy of Science, Szeged, Hungary Department of Applied Biotechnology and Food Sciences, University of Technology and Economics, Budapest, Hungary Cited By :49 Export Date: 10 May 2021 Correspondence Address: Vértessy, B. G.; Institute of Enzymology, , Budapest, Hungary; email: vertessy@enzim.hu Chemicals/CAS: DNA, 9007-49-2; deoxyuridine triphosphate pyrophosphatase, 37289-34-2; uracil, 66-22-8; inorganic pyrophosphatase, 9024-82-2, 9033-44-7; uracil DNA glycosidase, 59088-21-0; DNA, 9007-49-2; Pyrophosphatases, 3.6.1.-; Uracil, 66-22-8; Uracil-DNA Glycosidase, 3.2.2.-; dUTP pyrophosphatase, 3.6.1.23 Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Science, Budapest, Hungary Institute of Genetics, Biological Research Centre (BRC), Hungarian Academy of Science, Szeged, Hungary Department of Applied Biotechnology and Food Sciences, University of Technology and Economics, Budapest, Hungary Cited By :49 Export Date: 11 May 2021 Correspondence Address: Vértessy, B. G.; Institute of Enzymology, , Budapest, Hungary; email: vertessy@enzim.hu Chemicals/CAS: DNA, 9007-49-2; deoxyuridine triphosphate pyrophosphatase, 37289-34-2; uracil, 66-22-8; inorganic pyrophosphatase, 9024-82-2, 9033-44-7; uracil DNA glycosidase, 59088-21-0; DNA, 9007-49-2; Pyrophosphatases, 3.6.1.-; Uracil, 66-22-8; Uracil-DNA Glycosidase, 3.2.2.-; dUTP pyrophosphatase, 3.6.1.23 Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Science, Budapest, Hungary Institute of Genetics, Biological Research Centre (BRC), Hungarian Academy of Science, Szeged, Hungary Department of Applied Biotechnology and Food Sciences, University of Technology and Economics, Budapest, Hungary Cited By :49 Export Date: 12 May 2021 Correspondence Address: Vértessy, B. G.; Institute of Enzymology, , Budapest, Hungary; email: vertessy@enzim.hu Chemicals/CAS: DNA, 9007-49-2; deoxyuridine triphosphate pyrophosphatase, 37289-34-2; uracil, 66-22-8; inorganic pyrophosphatase, 9024-82-2, 9033-44-7; uracil DNA glycosidase, 59088-21-0; DNA, 9007-49-2; Pyrophosphatases, 3.6.1.-; Uracil, 66-22-8; Uracil-DNA Glycosidase, 3.2.2.-; dUTP pyrophosphatase, 3.6.1.23 Funding Agency and Grant Number: Hungarian Scientific Research FundOrszagos Tudomanyos Kutatasi Alapprogramok (OTKA) [OTKA K68229, NK84008, CK78646, K75774, NKTH-OTKA H07-BEL74200]; National Innovation Office; New Hungary Development Plan [TAMOP-4.2.1/B-09/1/KMR-2010-0002]; Howard Hughes Medical InstitutesHoward Hughes Medical Institute [55005628, 55000342]; Alexander von Humboldt-Stiftung, GermanyAlexander von Humboldt Foundation Funding text: This work was supported by the Hungarian Scientific Research Fund (OTKA K68229, NK84008, CK78646, K75774, NKTH-OTKA H07-BEL74200), the National Innovation Office, the New Hungary Development Plan (TAMOP-4.2.1/B-09/1/KMR-2010-0002), Howard Hughes Medical Institutes #55005628 and #55000342, and Alexander von Humboldt-Stiftung, Germany. The funders had no role in study design, data collection and analysis, decision to publish or preparation of the manuscript. AB - Base-excision repair and control of nucleotide pools safe-guard against permanent uracil accumulation in DNA relying on two key enzymes: uracil-DNA glycosylase and dUTPase. Lack of the major uracil-DNA glycosylase UNG gene from the fruit fly genome and dUTPase from fruit fly larvae prompted the hypotheses that i) uracil may accumulate in Drosophila genomic DNA where it may be well tolerated, and ii) this accumulation may affect development. Here we show that i) Drosophila melanogaster tolerates high levels of uracil in DNA; ii) such DNA is correctly interpreted in cell culture and embryo; and iii) under physiological spatio-temporal control, DNA from fruit fly larvae, pupae, and imago contain greatly elevated levels of uracil (200-2,000 uracil/million bases, quantified using a novel real-time PCR-based assay). Uracil is accumulated in genomic DNA of larval tissues during larval development, whereas DNA from imaginal tissues contains much less uracil. Upon pupation and metamorphosis, uracil content in DNA is significantly decreased. We propose that the observed developmental pattern of uracil-DNA is due to the lack of the key repair enzyme UNG from the Drosophila genome together with down-regulation of dUTPase in larval tissues. In agreement, we show that dUTPase silencing increases the uracil content in DNA of imaginal tissues and induces strong lethality at the early pupal stages, indicating that tolerance of highly uracil-substituted DNA is also stage-specific. Silencing of dUTPase perturbs the physiological pattern of uracil-DNA accumulation in Drosophila and leads to a strongly lethal phenotype in early pupal stages. These findings suggest a novel role of uracil-containing DNA in Drosophila development and metamorphosis and present a novel example for developmental effects of dUTPase silencing in multicellular eukaryotes. Importantly, we also show lack of the UNG gene in all available genomes of other Holometabola insects, indicating a potentially general tolerance and developmental role of uracil-DNA in this evolutionary clade. LA - English DB - MTMT ER - TY - JOUR AU - Virágh, Eszter Erika AU - Gorjánácz, Mátyás AU - Török, István AU - Eichhorn, T AU - Kallakuri, S AU - Szlanka, Tamás AU - Kiss, István AU - Mechler, BM TI - Specific Cooperation Between Imp­α2 and Imp­β/Ketel in Spindle assembly during Drosophila Early Nuclear Divisions JF - G3-GENES GENOMES GENETICS J2 - G3-GENES GENOM GENET VL - 2 PY - 2012 IS - 1 SP - 1 EP - 14 PG - 14 SN - 2160-1836 DO - 10.1534/g3.111.001073 UR - https://m2.mtmt.hu/api/publication/1922090 ID - 1922090 N1 - Megjegyzés-22392659 M1: Copyright (C) 2012 American Chemical Society (ACS). All Rights Reserved. CAPLUS AN 2012:524248(Journal; Online Computer File) Megjegyzés-23500598 FN: Thomson Reuters Web of Knowledge Department of Developmental Genetics, DKFZ-ZMBH Allianz, Heidelberg 69120, Germany Department of Pharmaceutical Biology, DKFZ-ZMBH Allianz, Heidelberg 69120, Germany Institute of Genetics, Biological Research Center, Hungarian Academy of Sciences, Szeged H-6726, Hungary Institute of Biochemistry, Biological Research Center, Hungarian Academy of Sciences, Szeged H-6726, Hungary European Molecular Biology Laboratory, 69117 Heidelberg, Germany Department of Pharmaceutical Biology, Institute of Pharmacy and Biochemistry, University of Mainz, 55128 Mainz, Germany Department of Genetics, Yale School of Medicine, New Haven, CT 06520, United States Charles University in Prague, First Faculty of Medicine, Albertov 4, 12800 Prague, Czech Republic VIT-University, Vellore, 632 014, Tamil Nadu, India Cited By :2 Export Date: 12 February 2021 Correspondence Address: Szlanka, T.; Institute of Genetics, Temesvári krt. 62, H-6726 Szeged, Hungary; email: szlanka@brc.hu Funding details: Deutsche Forschungsgemeinschaft, DFG, UNG 436 113/81/0-6 LA - English DB - MTMT ER - TY - JOUR AU - Chen, D AU - Ahlford, A AU - Schnorrer, F AU - Kalchhauser, I AU - Fellner, M AU - Virágh, Eszter Erika AU - Kiss, István AU - Syvanen, AC AU - Dickson, BJ TI - High-resolution, high-throughput SNP mapping in Drosophila melanogaster JF - NATURE METHODS J2 - NAT METHODS VL - 5 PY - 2008 IS - 4 SP - 323 EP - 329 PG - 7 SN - 1548-7091 DO - 10.1038/NMETH.1191 UR - https://m2.mtmt.hu/api/publication/1916849 ID - 1916849 N1 - Megjegyzés-22232548 Z9: 10 DI: 10.1038/NMETH.1191 AB - Single nucleotide polymorphisms (SNPs) are useful markers for genetic mapping experiments in model organisms. Here we report the establishment of a high-density SNP map and high-throughput genotyping assays for Drosophila melanogaster. Our map comprises 27,367 SNPs in common laboratory Drosophila stocks. These SNPs were clustered within 2,238 amplifiable markers at an average density of 1 marker every 50.3 kb, or 6.3 genes. We have also constructed a set of 62 Drosophila stocks, each of which facilitates the generation of recombinants within a defined genetic interval of 1-2 Mb. For flexible, high-throughput SNP genotyping, we used fluorescent tag-array mini-sequencing (TAMS) assays. We designed and validated TAMS assays for 293 SNPs at an average resolution of 391.3 kb, and demonstrated the utility of these tools by rapidly mapping 14 mutations that disrupt embryonic muscle patterning. These resources enable high-resolution high-throughput genetic mapping in Drosophila. LA - English DB - MTMT ER - TY - JOUR AU - Kiss, AS AU - Kiss, István AU - Csikkel-Szolnoki, A TI - The toxic effect of aluminium and its supposable mechanism in Drosophila JF - ACTA PHYTOPATHOLOGICA ET ENTOMOLOGICA HUNGARICA J2 - ACTA PHYTOPATHOL ENTOMOL HUNG VL - 12 PY - 2007 IS - 4 SP - 281 EP - 285 PG - 5 SN - 0238-1249 UR - https://m2.mtmt.hu/api/publication/1915394 ID - 1915394 LA - English DB - MTMT ER - TY - JOUR AU - Gorjánácz, Mátyás AU - Török, István AU - Pomozi, István AU - Garab, Győző AU - Szlanka, Tamás AU - Kiss, István AU - Mechler, BM TI - Domains of importin-alpha 2 required for ring canal assembly during Drosophila oogenesis JF - JOURNAL OF STRUCTURAL BIOLOGY J2 - J STRUCT BIOL VL - 154 PY - 2006 SP - 27 EP - 41 PG - 15 SN - 1047-8477 DO - 10.1016/j.jsb.2005.12.007 UR - https://m2.mtmt.hu/api/publication/1914423 ID - 1914423 LA - English DB - MTMT ER - TY - JOUR AU - Page, AR AU - Kovacs, A AU - Deák, Péter AU - Török, Tibor AU - Kiss, István AU - Dario, P AU - Bastos, C AU - Batista, P AU - Gomes, R AU - Ohkura, H AU - Russell, S AU - Glover, DM TI - Spotted-dick, a zinc-finger protein of Drosophila required for expression of Orc4 and S phase JF - EMBO JOURNAL J2 - EMBO J VL - 24 PY - 2005 SP - 4304 EP - 4315 PG - 12 SN - 0261-4189 DO - 10.1038/sj.emboj.7600890 UR - https://m2.mtmt.hu/api/publication/1914329 ID - 1914329 LA - English DB - MTMT ER - TY - JOUR AU - Szlanka, Tamás AU - Haracska, Lajos AU - Kiss, István AU - Deák, Péter AU - Kurucz, Judit Éva AU - Andó, István AU - Virágh, Eszter Erika AU - Udvardy, Andor TI - Deletion of proteasomal subunit S5a/Rpn10/p54 causes lethality, multiple mitotic defects and overexpression of proteasomal genes in Drosophila melanogaster JF - JOURNAL OF CELL SCIENCE J2 - J CELL SCI VL - 116 PY - 2003 IS - 6 SP - 1023 EP - 1033 PG - 11 SN - 0021-9533 DO - 10.1242/jcs.00332 UR - https://m2.mtmt.hu/api/publication/1912844 ID - 1912844 N1 - \n Cited By :48 \n Export Date: 1 December 2018 \n CODEN: JNCSA \n Correspondence Address: Udvardy, A.; Biol. Res. Ctr. Hungarian Acad. Sci., P.O. Box 521, H-6701 Szeged, Hungary; email: udvardy@nucleus.szbk.u-szeged.hu AB - The regulatory complex of the 26S proteasome is responsible for the selective recognition and binding of multiubiquitinated proteins. It was earlier shown that the subunit S5a/Rpn10/p54 of the regulatory complex is the only cellular protein capable of binding multiubiquitin chains in an in vitro overlay assay. The role of this subunit in substrate selection, however, is a subject of debate, following the observation that its deletion in Saccharomyces cerevisiae is not lethal and instead causes only a mild phenotype. To study the function of this subunit in higher eukaryotes, a mutant Drosophila strain was constructed by deleting the single copy gene encoding subunit S5a/Rpn10/p54. This deletion caused larval-pupal polyphasic lethality, multiple mitotic defects, the accumulation of higher multimers of ubiquitinated proteins and a huge accumulation of defective 26S proteasome particles. Deletion of the subunit S5a/Rpn10/p54 does not destabilise the regulatory complex and does not disturb the assembly of the regulatory complex and the catalytic core. The pupal lethality is a consequence of the depletion of the maternally provided 26S proteasome during the larval stages and a sudden increase in the proteasomal activity demands during the first few hours of pupal development. The huge accumulation of the fully assembled 26S proteasome in the deletion mutant and the lack of free subunits or partially assembled particles indicate that there is a highly coordinated accumulation of all the subunits of the 26S proteasome. This suggests that in higher eukaryotes, as with yeast, a feedback circuit coordinately regulates the expression of the proteasomal genes, and this adjusts the actual proteasome concentration in the cells according to the temporal and/or spatial proteolytic demands. LA - English DB - MTMT ER -