المؤلفون: E. N. Andreyeva, A. A. Ogienko, A. A. Yushkova, J. V. Popova, G. A. Pavlova, E. N. Kozhevnikova, A. V. Ivankin, M. Gatti, A. V. Pindyurin, Е. Н. Андреева, А. А. Огиенко, А. А. Юшкова, Ю. В. Попова, Г. А. Павлова, Е. Н. Кожевникова, А. В. Иванкин, М. Гатти, А. В. Пиндюрин

المصدر: Vavilov Journal of Genetics and Breeding; Том 23, № 2 (2019); 190-198 ; Вавиловский журнал генетики и селекции; Том 23, № 2 (2019); 190-198 ; 2500-3259 ; 2500-0462

مصطلحات موضوعية: биогенез рибосом, nucleolus, Minute-like phenotype, Non3, Fibrillarin, Rpf2, Brix domain, ribosome biogenesis, ядрышко, фенотип Minute-like, Brix домен

وصف الملف: application/pdf

Relation: https://vavilov.elpub.ru/jour/article/view/1935/1199; Biedka S., Micic J., Wilson D., Brown H., Diorio-Toth L., Wool- ford J.L., Jr. Hierarchical recruitment of ribosomal proteins and as-sembly factors remodels nucleolar pre-60S ribosomes. J. Cell Biol. 2018;217(7):2503-2518. DOI 10.1083/jcb.201711037.; Bischof J., Maeda R.K., Hediger M., Karch F., Basler K. An optimized transgenesis system for Drosophila using germ-line-specific фС31 integrases. Proc. Natl. Acad. Sci. USA. 2007;104(9):3312-3317. DOI 10.1073/pnas.06115nm4.; Bonaccorsi S., Giansanti M.G., Gatti M. Spindle assembly in Dro-sophila neuroblasts and ganglion mother cells. Nat. Cell Biol. 2000; 2(1):54-56. DOI 10.1038/71378.; Chalkley G.E., Verrijzer C.P. Immuno-depletion and purification strate¬gies to study chromatin-remodeling factors in vitro. Methods En- zymol. 2004;377:421-442. DOI 10.1016/S0076-6879(03)77028-1.; Cui Z., DiMario P.J. RNAi knockdown of Nopp140 induces Minute-like phenotypes in Drosophila. Mol. Biol. Cell. 2007;18(6):2179- 2191. DOI 10.1091/mbc.e07-01-0074.; Draptchinskaia N., Gustavsson P., Andersson B., Pettersson M., Wil- lig T.N., Dianzani I., Ball S., Tchernia G., Klar J., Matsson H., Tentler D., Mohandas N., Carlsson B., Dahl N. The gene encoding ribosomal protein S19 is mutated in Diamond-Blackfan anaemia. Nat. Genet. 1999;21(2):169-175. DOI 10.1038/5951.; Farley-Barnes K.I., McCann K.L., Ogawa L.M., Merkel J., Surov- tseva Y.V., Baserga S.J. Diverse regulators of human ribosome bio¬genesis discovered by changes in nucleolar number. Cell Rep. 2018; 22(7):1923-1934. DOI 10.1016/j.celrep.2018.01.056.; Fisher E.M.C., Beer-Romero P, Brown L.G., Ridley A., McNeil J.A., Lawrence J.B., Willard H.F., Bieber F.R., Page D.C. Homologous ribosomal protein genes on the human X and Y chromosomes: escape from X inactivation and possible implications for Turner syndrome. Cell. 1990;63(6):1205-1218.; Genuth N.R., Barna M. The discovery of ribosome heterogeneity and its implications for gene regulation and organismal life. Mol. Cell. 2018;71(3):364-374. DOI 10.1016/j.molcel.2018.07.018.; Goudarzi K.M., Lindstrom M.S. Role of ribosomal protein mutations in tumor development. Int. J. Oncol. 2016;48(4):1313-1324. DOI 10.3892/ijo.2016.3387.; Gramates L.S., Marygold S.J., Santos G.D., Urbano J.M., Antonazzo G., Matthews B.B., Rey A.J., Tabone C.J., Crosby M.A., Emmert D.B., Falls K., Goodman J.L., Hu Y., Ponting L., Schroeder A.J., Stre¬lets V.B., Thurmond J., Zhou P., the FlyBase Consortium. FlyBase at 25: looking to the future. Nucleic Acids Res. 2017;45(D1):D663- D671. DOI 10.1093/nar/gkw1016.; Gupta V, Warner J.R. Ribosome-omics of the human ribosome. RNA. 2014;20(7):1004-1013. DOI 10.1261/rna.043653.113.; Henras A.K., Plisson-Chastang C., O’Donohue M.F., Chakraborty A., Gleizes P.E. An overview of pre-ribosomal RNA processing in eukaryotes. Wiley Interdiscip. Rev. RNA. 2015;6(2):225-242. DOI 10.1002/wrna.1269.; Hoskins R.A., Carlson J.W., Wan K.H., Park S., Mendez I., Galle S.E., Booth B.W., Pfeiffer B.D., George R.A., Svirskas R., Krzywinski M., Schein J., Accardo M.C., Damia E., Messina G., Mendez-Lago M., de Pablos B., Demakova O.V., Andreyeva E.N., Boldyreva L.V., Marra M., Carvalho A.B., Dimitri P., Villasante A., Zhimulev I.F., Rubin G.M., Karpen G.H., Celniker S.E. The Release 6 reference sequence of the Drosophila melanogaster genome. Genome Res. 2015;25(3):445-458. DOI 10.1101/gr.185579.114.; Huang W., Massouras A., Inoue Y., Peiffer J., Ramia M., Tarone A.M., Turlapati L., Zichner T., Zhu D., Lyman R.F., Magwire M.M., Blankenburg K., Carbone M.A., Chang K., Ellis L.L., Fernan¬dez S., Han Y., Highnam G., Hjelmen C.E., Jack J.R., Javaid M., Jayaseelan J., Kalra D., Lee S., Lewis L., Munidasa M., Ongeri F., Patel S., Perales L., Perez A., Pu L., Rollmann S.M., Ruth R., Saa- da N., Warner C., Williams A., Wu Y.Q., Yamamoto A., Zhang Y., Zhu Y., Anholt R.R., Korbel J.O., Mittelman D., Muzny D.M., Gibbs R.A., Barbadilla A., Johnston J.S., Stone E.A., Richards S., Deplancke B., Mackay T.F.C. Natural variation in genome architec¬ture among 205 Drosophila melanogaster Genetic Reference Panel lines. Genome Res. 2014;24(7):1193-1208. DOI 10.1101/gr.171546. 113.; Kearse M.G., Chen A.S., Ware V.C. Expression of ribosomal protein L22e family members in Drosophila melanogaster: rpL22-like is differentially expressed and alternatively spliced. Nucleic Acids Res. 2011;39(7):2701-2716. DOI 10.1093/nar/gkq1218.; Kongsuwan K., Yu Q., Vincent A., Frisardi M.C., Rosbash M., Len- gyel J.A., Merriam J. A Drosophila Minute gene encodes a ribo-somal protein. Nature. 1985;317(6037):555-558.; Kressler D., Hurt E., Bafiler J. A puzzle of life: crafting ribosomal sub¬units. Trends Biochem. Sci. 2017;42(8):640-654. DOI 10.1016/j. tibs.2017.05.005.; Lopes A.M., Miguel R.N., Sargent C.A., Ellis P.J., Amorim A., Af- fara N.A. The human RPS4 paralogue on Yq11.223 encodes a structurally conserved ribosomal protein and is preferentially ex-pressed during spermatogenesis. BMC Mol. Biol. 2010;11:33. DOI 10.1186/1471-2199-11-33.; Mackay T.F., Richards S., Stone E.A., Barbadilla A., Ayroles J.F., Zhu D., Casillas S., Han Y., Magwire M.M., Cridland J.M., Richard¬son M.F., Anholt R.R., Barron M., Bess C., Blankenburg K.P., Carbone M.A., Castellano D., Chaboub L., Duncan L., Harris Z., Javaid M., Jayaseelan J.C., Jhangiani S.N., Jordan K.W., Lara F., Lawrence F., Lee S.L., Librado P, Linheiro R.S., Lyman R.F., Mac¬key A.J., Munidasa M., Muzny D.M., Nazareth L., Newsham I., Pe¬rales L., Pu L.L., Qu C., Ramia M., Reid J.G., Rollmann S.M., Ro¬zas J., Saada N., Turlapati L., Worley K.C., Wu Y.Q., Yamamoto A., Zhu Y., Bergman C.M., Thornton K.R., Mittelman D., Gibbs R.A. The Drosophila melanogaster Genetic Reference Panel. Nature. 2012;482(7384):173-178. DOI 10.1038/nature10811.; Markstein M., Pitsouli C., Villalta C., Celniker S.E., Perrimon N. Ex-ploiting position effects and the gypsy retrovirus insulator to engineer precisely expressed transgenes. Nat. Genet. 2008;40(4):476- 483. DOI 10.1038/ng.101.; Marygold S.J., Coelho C.M.A., Leevers S.J. Genetic analysis of RpL38 and RpL5, two Minute genes located in the centric hetero-chromatin of chromosome 2 of Drosophila melanogaster. Genetics. 2005;169(2):683-695. DOI 10.1534/genetics.104.034124.; Marygold S.J., Roote J., Reuter G., Lambertsson A., Ashburner M., Millburn G.H., Harrison P.M., Yu Z., Kenmochi N., Kaufman T.C., Leevers S.J., Cook K.R. The ribosomal protein genes and Minute loci of Drosophila melanogaster. Genome Biol. 2007;8(10):R216. DOI 10.1186/gb-2007-8-10-r216.; Mills E.W., Green R. Ribosomopathies: there’s strength in numbers. Science. 2017;358(6363):eaan2755. DOI 10.1126/science.aan2755.; Morata G., Ripoll P. Minutes: mutants of Drosophila autonomously affecting cell division rate. Dev. Biol. 1975;42(2):211-221.; Moutinho-Pereira S., Stuurman N., Afonso O., Hornsveld M., Aguiar P., Goshima G., Vale R.D., Maiato H. Genes involved in centrosome- independent mitotic spindle assembly in Drosophila S2 cells. Proc. Natl. Acad. Sci. USA. 2013;110(49):19808-19813. DOI 10.1073/ pnas.1320013110.; Narla A., Ebert B.L. Ribosomopathies: human disorders of ribo¬some dysfunction. Blood. 2010;115(16):3196-3205. DOI 10.1182/ blood-2009-10-178129.; Neumuller R.A., Gross T., Samsonova A.A., Vinayagam A., Buck¬ner M., Founk K., Hu Y., Sharifpoor S., Rosebrock A.P., Andrews B., Winston F., Perrimon N. Conserved regulators of nucleolar size re¬vealed by global phenotypic analyses. Sci. Signal. 2013;6(289):ra70. DOI 10.1126/scisignal.2004145.; NMez Villacis L., Wong M.S., Ferguson L.L., Hein N., George A.J., Hannan K.M. New roles for the nucleolus in health and disease. BioEssays. 2018;40(5):e1700233. DOI 10.1002/bies.201700233.; O’Brochta D.A., Gomez S.P., Handler A.M. P element excision in Dro¬sophila melanogaster and related drosophilids. Mol. Gen. Genet. 1991;225(3):387-394.; Ogienko A.A., Yarinich L.A., Fedorova E.V., Lebedev M.O., Andrey-eva E.N., Pindyurin A.V., Baricheva E.M. New slbo-Gal4 driver lines for the analysis of border cell migration during Drosophi¬la oogenesis. Chromosoma. 2018;127(4):475-487. DOI 10.1007/ s00412-018-0676-7.; Olson M.O.J. Sensing cellular stress: another new function for the nucleolus? Sci. STKE. 2004;2004(224):pe10. DOI 10.1126/stke. 2242004pe10.; Pederson T. The plurifunctional nucleolus. Nucleic Acids Res. 1998; 26(17):3871-3876.; Robertson H.M., Preston C.R., Phillis R.W., Johnson-Schlitz D.M., Benz W.K., Engels W.R. A stable genomic source ofP element trans- posase in Drosophilamelanogaster. Genetics. 1988;118(3):461-470.; Rodriguez-Corona U., Sobol M., Rodriguez-Zapata L.C., Hozak P., Castano E. Fibrillarin from Archaea to human. Biol. Cell. 2015; 107(6):159-174. DOI 10.1111/boc.201400077.; Shi Z., Barna M. Translating the genome in time and space: spe-cialized ribosomes, RNA regulons, and RNA-binding proteins. Annu. Rev. Cell Dev. Biol. 2015;31:31-54. DOI 10.1146/annurev- cellbio-100814-125346.; Somma M.P., Ceprani F., Bucciarelli E., Naim V., De Arcangelis V., Piergentili R., Palena A., Ciapponi L., Giansanti M.G., Pellacani C., Petrucci R., Cenci G., Verni F., Fasulo B., Goldberg M.L., Di Cun- to F., Gatti M. Identification of Drosophila mitotic genes by com-bining co-expression analysis and RNA interference. PLoS Genet. 2008;4(7):e1000126. DOI 10.1371/journal.pgen.1000126.; Somma M.P., Fasulo B., Cenci G., Cundari E., Gatti M. Molecular dissection of cytokinesis by RNA interference in Drosophila cultured cells. Mol. Biol. Cell. 2002;13(7):2448-2460. DOI 10.1091/mbc.01- 12-0589.; Stage D.E., Eickbush T.H. Sequence variation within the rRNA gene loci of 12 Drosophila species. Genome Res. 2007;17(12):1888- 1897. DOI 10.1101/gr.6376807.; Strunov A., Boldyreva L.V., Pavlova G.A., Pindyurin A.V., Gatti M., Kiseleva E. A simple and effective method for ultrastructural analy¬sis of mitosis in Drosophila S2 cells. MethodsX. 2016;3:551-559. DOI 10.1016/j.mex.2016.10.003.; Tavares A.A.M., Glover D.M., Sunkel C.E. The conserved mitotic ki-nase polo is regulated by phosphorylation and has preferred microtubule-associated substrates in Drosophila embryo extracts. EMBO J. 1996;15(18):4873-4883.; Tutuncuoglu B., Jakovljevic J., Wu S., Gao N., Woolford J.L., Jr. The N-terminal extension of yeast ribosomal protein L8 is involved in two major remodeling events during late nuclear stages of 60S ri- bosomal subunit assembly. RNA. 2016;22(9):1386-1399. DOI 10.1261/rna.055798.115.; van Nues R.W., Watkins N.J. Unusual C'/D' motifs enable box C/D snoRNPs to modify multiple sites in the same rRNA target region. Nucleic Acids Res. 2017;45(4):2016-2028.; Wehner K.A., Baserga S.J. The o70-like motif: a eukaryotic RNA binding domain unique to a superfamily of proteins required for ribosome biogenesis. Mol. Cell. 2002;9(2):329-339. DOI 10.1016/ S1097-2765(02)00438-0.; Xue S., Barna M. Specialized ribosomes: a new frontier in gene regula¬tion and organismal biology. Nat. Rev. Mol. Cell Biol. 2012;13(6): 355-369. DOI 10.1038/nrm3359.; Yang X., Mao F., Lv X., Zhang Z., Fu L., Lu Y., Wu W., Zhou Z., Zhang L., Zhao Y. Drosophila Vps36 regulates Smo trafficking in Hedgehog signaling. J. Cell Sci. 2013;126(Pt.18):4230-4238. DOI 10.1242/jcs.128603.; Zhang J., Harnpicharnchai P., Jakovljevic J., Tang L., Guo Y., Oeffin- ger M., Rout M.P., Hiley S.L., Hughes T., Woolford J.L., Jr. Assembly factors Rpf2 and Rrs1 recruit 5S rRNA and ribosomal proteins rpL5 and rpL11 into nascent ribosomes. Genes Dev. 2007;21(20):2580- 2592. DOI 10.1101/gad.1569307.; https://vavilov.elpub.ru/jour/article/view/1935

الاتاحة: https://vavilov.elpub.ru/jour/article/view/1935
https://doi.org/10.18699/VJ19.481