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dc.contributor.author | Poidevin, Laetitia![]() |
es_ES |
dc.contributor.author | Unal, Dilek![]() |
es_ES |
dc.contributor.author | Belda-Palazón, Borja![]() |
es_ES |
dc.contributor.author | Ferrando Monleón, Alejandro Ramón![]() |
es_ES |
dc.date.accessioned | 2021-02-02T04:32:35Z | |
dc.date.available | 2021-02-02T04:32:35Z | |
dc.date.issued | 2019-04 | es_ES |
dc.identifier.uri | http://hdl.handle.net/10251/160424 | |
dc.description.abstract | [EN] Plant polyamines (PAs) have been assigned a large number of physiological functions with unknown molecular mechanisms in many cases. Among the most abundant and studied polyamines, two of them, namely spermidine (Spd) and thermospermine (Tspm), share some molecular functions related to quality control pathways for tightly regulated mRNAs at the level of translation. In this review, we focus on the roles of Tspm and Spd to facilitate the translation of mRNAs containing upstream ORFs (uORFs), premature stop codons, and ribosome stalling sequences that may block translation, thus preventing their degradation by quality control mechanisms such as the nonsense-mediated decay pathway and possible interactions with other mRNA quality surveillance pathways. | es_ES |
dc.description.sponsorship | A.F. was funded by the Spanish Ministry of Science, Innovation and Universities, grant number BIO2015-70483-R, and B.B.-P. was funded by the Generalitat Valenciana grant, VALi+d GVA APOSTD/2017/039. D.U. was a recipient of an EMBO short-term fellowship, number STF-7308. | es_ES |
dc.language | Inglés | es_ES |
dc.publisher | MDPI | es_ES |
dc.relation.ispartof | Plants | es_ES |
dc.rights | Reconocimiento (by) | es_ES |
dc.subject | Polyamines | es_ES |
dc.subject | Spermidine | es_ES |
dc.subject | Thermospermine | es_ES |
dc.subject | Nonsense-mediated decay | es_ES |
dc.subject | No-go decay | es_ES |
dc.subject | Non-stop decay | es_ES |
dc.subject | Quality control | es_ES |
dc.subject | Translation | es_ES |
dc.title | Polyamines as Quality Control Metabolites Operating at the Post-Transcriptional Level | es_ES |
dc.type | Artículo | es_ES |
dc.identifier.doi | 10.3390/plants8040109 | es_ES |
dc.relation.projectID | info:eu-repo/grantAgreement/MINECO//BIO2015-70483-R/ES/PAPEL DE LA ESPERMIDINA Y DE LA BIOSINTESIS DE PROTEINAS EN LA TOLERANCIA DEL POLEN A LAS ALTAS TEMPERATURAS/ | es_ES |
dc.relation.projectID | info:eu-repo/grantAgreement/GVA//APOSTD%2F2017%2F039/ | es_ES |
dc.relation.projectID | info:eu-repo/grantAgreement/EMBO//STF-7308/ | es_ES |
dc.rights.accessRights | Abierto | es_ES |
dc.contributor.affiliation | Universitat Politècnica de València. Instituto Universitario Mixto de Biología Molecular y Celular de Plantas - Institut Universitari Mixt de Biologia Molecular i Cel·lular de Plantes | es_ES |
dc.description.bibliographicCitation | Poidevin, L.; Unal, D.; Belda-Palazón, B.; Ferrando Monleón, AR. (2019). Polyamines as Quality Control Metabolites Operating at the Post-Transcriptional Level. Plants. 8(4):1-13. https://doi.org/10.3390/plants8040109 | es_ES |
dc.description.accrualMethod | S | es_ES |
dc.relation.publisherversion | https://doi.org/10.3390/plants8040109 | es_ES |
dc.description.upvformatpinicio | 1 | es_ES |
dc.description.upvformatpfin | 13 | es_ES |
dc.type.version | info:eu-repo/semantics/publishedVersion | es_ES |
dc.description.volume | 8 | es_ES |
dc.description.issue | 4 | es_ES |
dc.identifier.eissn | 2223-7747 | es_ES |
dc.identifier.pmid | 31022874 | es_ES |
dc.identifier.pmcid | PMC6524035 | es_ES |
dc.relation.pasarela | S\406565 | es_ES |
dc.contributor.funder | Ministerio de Economía, Industria y Competitividad | es_ES |
dc.contributor.funder | Generalitat Valenciana | es_ES |
dc.contributor.funder | European Molecular Biology Organization | es_ES |
dc.description.references | Graille, M., & Séraphin, B. (2012). Surveillance pathways rescuing eukaryotic ribosomes lost in translation. Nature Reviews Molecular Cell Biology, 13(11), 727-735. doi:10.1038/nrm3457 | es_ES |
dc.description.references | Preissler, S., & Deuerling, E. (2012). Ribosome-associated chaperones as key players in proteostasis. Trends in Biochemical Sciences, 37(7), 274-283. doi:10.1016/j.tibs.2012.03.002 | es_ES |
dc.description.references | Fuell, C., Elliott, K. A., Hanfrey, C. C., Franceschetti, M., & Michael, A. J. (2010). Polyamine biosynthetic diversity in plants and algae. Plant Physiology and Biochemistry, 48(7), 513-520. doi:10.1016/j.plaphy.2010.02.008 | es_ES |
dc.description.references | Vera-Sirera, F., Minguet, E. G., Singh, S. K., Ljung, K., Tuominen, H., Blázquez, M. A., & Carbonell, J. (2010). Role of polyamines in plant vascular development. Plant Physiology and Biochemistry, 48(7), 534-539. doi:10.1016/j.plaphy.2010.01.011 | es_ES |
dc.description.references | IGARASHI, K., SUGAWARA, K., IZUMI, I., NAGAYAMA, C., & HIROSE, S. (1974). Effect of Polyamines on Polyphenylalanine Synthesis by Escherichia coli and Rat-Liver Ribosomes. European Journal of Biochemistry, 48(2), 495-502. doi:10.1111/j.1432-1033.1974.tb03790.x | es_ES |
dc.description.references | IGARASHI, K., HASHIMOTO, S., MIYAKE, A., KASHIWAGI, K., & HIROSE, S. (2005). Increase of Fidelity of Polypeptide Synthesis by Spermidine in Eukaryotic Cell-Free Systems. European Journal of Biochemistry, 128(2-3), 597-604. doi:10.1111/j.1432-1033.1982.tb07006.x | es_ES |
dc.description.references | Echandi, G., & Algranati, I. D. (1975). Defective 30S ribosomal particles in a polyamine auxotroph of Escherichia coli. Biochemical and Biophysical Research Communications, 67(3), 1185-1191. doi:10.1016/0006-291x(75)90798-6 | es_ES |
dc.description.references | Igarashi, K., Kishida, K., & Hirose, S. (1980). Stimulation by polyamines of enzymatic methylation of two adjacent adenines near the 3′ end of 16S ribosomal RNA of Escherichia coli. Biochemical and Biophysical Research Communications, 96(2), 678-684. doi:10.1016/0006-291x(80)91408-4 | es_ES |
dc.description.references | Hetrick, B., Khade, P. K., Lee, K., Stephen, J., Thomas, A., & Joseph, S. (2010). Polyamines Accelerate Codon Recognition by Transfer RNAs on the Ribosome. Biochemistry, 49(33), 7179-7189. doi:10.1021/bi1009776 | es_ES |
dc.description.references | Amarantos, I. (2000). Photoaffinity polyamines: interactions with AcPhe-tRNA free in solution or bound at the P-site of Escherichia coli ribosomes. Nucleic Acids Research, 28(19), 3733-3742. doi:10.1093/nar/28.19.3733 | es_ES |
dc.description.references | Amarantos, I. (2002). The identification of spermine binding sites in 16S rRNA allows interpretation of the spermine effect on ribosomal 30S subunit functions. Nucleic Acids Research, 30(13), 2832-2843. doi:10.1093/nar/gkf404 | es_ES |
dc.description.references | Xaplanteri, M. A. (2005). Localization of spermine binding sites in 23S rRNA by photoaffinity labeling: parsing the spermine contribution to ribosomal 50S subunit functions. Nucleic Acids Research, 33(9), 2792-2805. doi:10.1093/nar/gki557 | es_ES |
dc.description.references | Dever, T. E., & Ivanov, I. P. (2018). Roles of polyamines in translation. Journal of Biological Chemistry, 293(48), 18719-18729. doi:10.1074/jbc.tm118.003338 | es_ES |
dc.description.references | Ivanov, I. P. (2000). Conservation of polyamine regulation by translational frameshifting from yeast to mammals. The EMBO Journal, 19(8), 1907-1917. doi:10.1093/emboj/19.8.1907 | es_ES |
dc.description.references | Brandman, O., & Hegde, R. S. (2016). Ribosome-associated protein quality control. Nature Structural & Molecular Biology, 23(1), 7-15. doi:10.1038/nsmb.3147 | es_ES |
dc.description.references | Behm-Ansmant, I., Kashima, I., Rehwinkel, J., Saulière, J., Wittkopp, N., & Izaurralde, E. (2007). mRNA quality control: An ancient machinery recognizes and degrades mRNAs with nonsense codons. FEBS Letters, 581(15), 2845-2853. doi:10.1016/j.febslet.2007.05.027 | es_ES |
dc.description.references | Chang, Y.-F., Imam, J. S., & Wilkinson, M. F. (2007). The Nonsense-Mediated Decay RNA Surveillance Pathway. Annual Review of Biochemistry, 76(1), 51-74. doi:10.1146/annurev.biochem.76.050106.093909 | es_ES |
dc.description.references | Brogna, S., & Wen, J. (2009). Nonsense-mediated mRNA decay (NMD) mechanisms. Nature Structural & Molecular Biology, 16(2), 107-113. doi:10.1038/nsmb.1550 | es_ES |
dc.description.references | Amrani, N., Sachs, M. S., & Jacobson, A. (2006). Early nonsense: mRNA decay solves a translational problem. Nature Reviews Molecular Cell Biology, 7(6), 415-425. doi:10.1038/nrm1942 | es_ES |
dc.description.references | Rebbapragada, I., & Lykke-Andersen, J. (2009). Execution of nonsense-mediated mRNA decay: what defines a substrate? Current Opinion in Cell Biology, 21(3), 394-402. doi:10.1016/j.ceb.2009.02.007 | es_ES |
dc.description.references | Peccarelli, M., & Kebaara, B. W. (2014). Regulation of Natural mRNAs by the Nonsense-Mediated mRNA Decay Pathway. Eukaryotic Cell, 13(9), 1126-1135. doi:10.1128/ec.00090-14 | es_ES |
dc.description.references | Kurihara, Y., Matsui, A., Hanada, K., Kawashima, M., Ishida, J., Morosawa, T., … Seki, M. (2009). Genome-wide suppression of aberrant mRNA-like noncoding RNAs by NMD in Arabidopsis. Proceedings of the National Academy of Sciences, 106(7), 2453-2458. doi:10.1073/pnas.0808902106 | es_ES |
dc.description.references | Drechsel, G., Kahles, A., Kesarwani, A. K., Stauffer, E., Behr, J., Drewe, P., … Wachter, A. (2013). Nonsense-Mediated Decay of Alternative Precursor mRNA Splicing Variants Is a Major Determinant of the Arabidopsis Steady State Transcriptome. The Plant Cell, 25(10), 3726-3742. doi:10.1105/tpc.113.115485 | es_ES |
dc.description.references | Kalyna, M., Simpson, C. G., Syed, N. H., Lewandowska, D., Marquez, Y., Kusenda, B., … Brown, J. W. S. (2011). Alternative splicing and nonsense-mediated decay modulate expression of important regulatory genes in Arabidopsis. Nucleic Acids Research, 40(6), 2454-2469. doi:10.1093/nar/gkr932 | es_ES |
dc.description.references | Leeds, P., Wood, J. M., Lee, B. S., & Culbertson, M. R. (1992). Gene products that promote mRNA turnover in Saccharomyces cerevisiae. Molecular and Cellular Biology, 12(5), 2165-2177. doi:10.1128/mcb.12.5.2165 | es_ES |
dc.description.references | Kerényi, Z., Mérai, Z., Hiripi, L., Benkovics, A., Gyula, P., Lacomme, C., … Silhavy, D. (2008). Inter-kingdom conservation of mechanism of nonsense-mediated mRNA decay. The EMBO Journal, 27(11), 1585-1595. doi:10.1038/emboj.2008.88 | es_ES |
dc.description.references | Shaul, O. (2015). Unique Aspects of Plant Nonsense-Mediated mRNA Decay. Trends in Plant Science, 20(11), 767-779. doi:10.1016/j.tplants.2015.08.011 | es_ES |
dc.description.references | Rayson, S., Arciga-Reyes, L., Wootton, L., De Torres Zabala, M., Truman, W., Graham, N., … Davies, B. (2012). A Role for Nonsense-Mediated mRNA Decay in Plants: Pathogen Responses Are Induced in Arabidopsis thaliana NMD Mutants. PLoS ONE, 7(2), e31917. doi:10.1371/journal.pone.0031917 | es_ES |
dc.description.references | Shi, C., Baldwin, I. T., & Wu, J. (2012). Arabidopsis Plants Having Defects in Nonsense-mediated mRNA Decay Factors UPF1, UPF2, and UPF3 Show Photoperiod-dependent Phenotypes in Development and Stress Responses. Journal of Integrative Plant Biology, 54(2), 99-114. doi:10.1111/j.1744-7909.2012.01093.x | es_ES |
dc.description.references | Nasim, Z., Fahim, M., & Ahn, J. H. (2017). Possible Role of MADS AFFECTING FLOWERING 3 and B-BOX DOMAIN PROTEIN 19 in Flowering Time Regulation of Arabidopsis Mutants with Defects in Nonsense-Mediated mRNA Decay. Frontiers in Plant Science, 8. doi:10.3389/fpls.2017.00191 | es_ES |
dc.description.references | Degtiar, E., Fridman, A., Gottlieb, D., Vexler, K., Berezin, I., Farhi, R., … Shaul, O. (2015). The feedback control of UPF3 is crucial for RNA surveillance in plants. Nucleic Acids Research, 43(8), 4219-4235. doi:10.1093/nar/gkv237 | es_ES |
dc.description.references | Popp, M. W.-L., & Maquat, L. E. (2013). Organizing Principles of Mammalian Nonsense-Mediated mRNA Decay. Annual Review of Genetics, 47(1), 139-165. doi:10.1146/annurev-genet-111212-133424 | es_ES |
dc.description.references | Dai, Y., Li, W., & An, L. (2015). NMD mechanism and the functions of Upf proteins in plant. Plant Cell Reports, 35(1), 5-15. doi:10.1007/s00299-015-1867-9 | es_ES |
dc.description.references | Karousis, E. D., & Mühlemann, O. (2018). Nonsense-Mediated mRNA Decay Begins Where Translation Ends. Cold Spring Harbor Perspectives in Biology, 11(2), a032862. doi:10.1101/cshperspect.a032862 | es_ES |
dc.description.references | Doma, M. K., & Parker, R. (2006). Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation elongation. Nature, 440(7083), 561-564. doi:10.1038/nature04530 | es_ES |
dc.description.references | Atkinson, G. C., Baldauf, S. L., & Hauryliuk, V. (2008). Evolution of nonstop, no-go and nonsense-mediated mRNA decay and their termination factor-derived components. BMC Evolutionary Biology, 8(1), 290. doi:10.1186/1471-2148-8-290 | es_ES |
dc.description.references | Szádeczky-Kardoss, I., Gál, L., Auber, A., Taller, J., & Silhavy, D. (2018). The No-go decay system degrades plant mRNAs that contain a long A-stretch in the coding region. Plant Science, 275, 19-27. doi:10.1016/j.plantsci.2018.07.008 | es_ES |
dc.description.references | Shoemaker, C. J., Eyler, D. E., & Green, R. (2010). Dom34:Hbs1 Promotes Subunit Dissociation and Peptidyl-tRNA Drop-Off to Initiate No-Go Decay. Science, 330(6002), 369-372. doi:10.1126/science.1192430 | es_ES |
dc.description.references | Tsuboi, T., Kuroha, K., Kudo, K., Makino, S., Inoue, E., Kashima, I., & Inada, T. (2012). Dom34:Hbs1 Plays a General Role in Quality-Control Systems by Dissociation of a Stalled Ribosome at the 3′ End of Aberrant mRNA. Molecular Cell, 46(4), 518-529. doi:10.1016/j.molcel.2012.03.013 | es_ES |
dc.description.references | Buchan, J. R., & Stansfield, I. (2007). Halting a cellular production line: responses to ribosomal pausing during translation. Biology of the Cell, 99(9), 475-487. doi:10.1042/bc20070037 | es_ES |
dc.description.references | Simms, C. L., Yan, L. L., & Zaher, H. S. (2017). Ribosome Collision Is Critical for Quality Control during No-Go Decay. Molecular Cell, 68(2), 361-373.e5. doi:10.1016/j.molcel.2017.08.019 | es_ES |
dc.description.references | Ozsolak, F., Kapranov, P., Foissac, S., Kim, S. W., Fishilevich, E., Monaghan, A. P., … Milos, P. M. (2010). Comprehensive Polyadenylation Site Maps in Yeast and Human Reveal Pervasive Alternative Polyadenylation. Cell, 143(6), 1018-1029. doi:10.1016/j.cell.2010.11.020 | es_ES |
dc.description.references | Dimitrova, L. N., Kuroha, K., Tatematsu, T., & Inada, T. (2009). Nascent Peptide-dependent Translation Arrest Leads to Not4p-mediated Protein Degradation by the Proteasome. Journal of Biological Chemistry, 284(16), 10343-10352. doi:10.1074/jbc.m808840200 | es_ES |
dc.description.references | Koutmou, K. S., Schuller, A. P., Brunelle, J. L., Radhakrishnan, A., Djuranovic, S., & Green, R. (2015). Ribosomes slide on lysine-encoding homopolymeric A stretches. eLife, 4. doi:10.7554/elife.05534 | es_ES |
dc.description.references | Van Hoof, A., Frischmeyer, P. A., Dietz, H. C., & Parker, R. (2002). Exosome-Mediated Recognition and Degradation of mRNAs Lacking a Termination Codon. Science, 295(5563), 2262-2264. doi:10.1126/science.1067272 | es_ES |
dc.description.references | Frischmeyer, P. A., van Hoof, A., O’Donnell, K., Guerrerio, A. L., Parker, R., & Dietz, H. C. (2002). An mRNA Surveillance Mechanism That Eliminates Transcripts Lacking Termination Codons. Science, 295(5563), 2258-2261. doi:10.1126/science.1067338 | es_ES |
dc.description.references | Szádeczky-Kardoss, I., Csorba, T., Auber, A., Schamberger, A., Nyikó, T., Taller, J., … Silhavy, D. (2018). The nonstop decay and the RNA silencing systems operate cooperatively in plants. Nucleic Acids Research, 46(9), 4632-4648. doi:10.1093/nar/gky279 | es_ES |
dc.description.references | Hanzawa, Y., Takahashi, T., & Komeda, Y. (1997). ACL5: an Arabidopsis gene required for internodal elongation after flowering. The Plant Journal, 12(4), 863-874. doi:10.1046/j.1365-313x.1997.12040863.x | es_ES |
dc.description.references | Hanzawa, Y. (2000). ACAULIS5, an Arabidopsis gene required for stem elongation, encodes a spermine synthase. The EMBO Journal, 19(16), 4248-4256. doi:10.1093/emboj/19.16.4248 | es_ES |
dc.description.references | Knott, J. M., Römer, P., & Sumper, M. (2007). Putative spermine synthases fromThalassiosira pseudonanaandArabidopsis thalianasynthesize thermospermine rather than spermine. FEBS Letters, 581(16), 3081-3086. doi:10.1016/j.febslet.2007.05.074 | es_ES |
dc.description.references | Minguet, E. G., Vera-Sirera, F., Marina, A., Carbonell, J., & Blazquez, M. A. (2008). Evolutionary Diversification in Polyamine Biosynthesis. Molecular Biology and Evolution, 25(10), 2119-2128. doi:10.1093/molbev/msn161 | es_ES |
dc.description.references | Milhinhos, A., Prestele, J., Bollhöner, B., Matos, A., Vera-Sirera, F., Rambla, J. L., … Miguel, C. M. (2013). Thermospermine levels are controlled by an auxin-dependent feedback loop mechanism inPopulusxylem. The Plant Journal, 75(4), 685-698. doi:10.1111/tpj.12231 | es_ES |
dc.description.references | Baima, S., Forte, V., Possenti, M., Peñalosa, A., Leoni, G., Salvi, S., … Morelli, G. (2014). Negative Feedback Regulation of Auxin Signaling by ATHB8/ACL5–BUD2 Transcription Module. Molecular Plant, 7(6), 1006-1025. doi:10.1093/mp/ssu051 | es_ES |
dc.description.references | Kakehi, J. -i., Kuwashiro, Y., Niitsu, M., & Takahashi, T. (2008). Thermospermine is Required for Stem Elongation in Arabidopsis thaliana. Plant and Cell Physiology, 49(9), 1342-1349. doi:10.1093/pcp/pcn109 | es_ES |
dc.description.references | Clay, N. K., & Nelson, T. (2005). Arabidopsis thickvein Mutation Affects Vein Thickness and Organ Vascularization, and Resides in a Provascular Cell-Specific Spermine Synthase Involved in Vein Definition and in Polar Auxin Transport. Plant Physiology, 138(2), 767-777. doi:10.1104/pp.104.055756 | es_ES |
dc.description.references | Muñiz, L., Minguet, E. G., Singh, S. K., Pesquet, E., Vera-Sirera, F., Moreau-Courtois, C. L., … Tuominen, H. (2008). ACAULIS5 controls Arabidopsis xylem specification through the prevention of premature cell death. Development, 135(15), 2573-2582. doi:10.1242/dev.019349 | es_ES |
dc.description.references | Imai, A., Hanzawa, Y., Komura, M., Yamamoto, K. T., Komeda, Y., & Takahashi, T. (2006). The dwarf phenotype of the Arabidopsis acl5 mutant is suppressed by a mutation in an upstream ORF of a bHLH gene. Development, 133(18), 3575-3585. doi:10.1242/dev.02535 | es_ES |
dc.description.references | Imai, A., Komura, M., Kawano, E., Kuwashiro, Y., & Takahashi, T. (2008). A semi-dominant mutation in the ribosomal protein L10 gene suppresses the dwarf phenotype of theacl5mutant inArabidopsis thaliana. The Plant Journal, 56(6), 881-890. doi:10.1111/j.1365-313x.2008.03647.x | es_ES |
dc.description.references | Kakehi, J.-I., Kawano, E., Yoshimoto, K., Cai, Q., Imai, A., & Takahashi, T. (2015). Mutations in Ribosomal Proteins, RPL4 and RACK1, Suppress the Phenotype of a Thermospermine-Deficient Mutant of Arabidopsis thaliana. PLOS ONE, 10(1), e0117309. doi:10.1371/journal.pone.0117309 | es_ES |
dc.description.references | Cai, Q., Fukushima, H., Yamamoto, M., Ishii, N., Sakamoto, T., Kurata, T., … Takahashi, T. (2016). TheSAC51Family Plays a Central Role in Thermospermine Responses in Arabidopsis. Plant and Cell Physiology, 57(8), 1583-1592. doi:10.1093/pcp/pcw113 | es_ES |
dc.description.references | Vera-Sirera, F., De Rybel, B., Úrbez, C., Kouklas, E., Pesquera, M., Álvarez-Mahecha, J. C., … Blázquez, M. A. (2015). A bHLH-Based Feedback Loop Restricts Vascular Cell Proliferation in Plants. Developmental Cell, 35(4), 432-443. doi:10.1016/j.devcel.2015.10.022 | es_ES |
dc.description.references | Yamamoto, M., & Takahashi, T. (2017). Thermospermine enhances translation of SAC51 and SACL1 in Arabidopsis. Plant Signaling & Behavior, 12(1), e1276685. doi:10.1080/15592324.2016.1276685 | es_ES |
dc.description.references | Von Arnim, A. G., Jia, Q., & Vaughn, J. N. (2014). Regulation of plant translation by upstream open reading frames. Plant Science, 214, 1-12. doi:10.1016/j.plantsci.2013.09.006 | es_ES |
dc.description.references | Weiss, M. C., Sousa, F. L., Mrnjavac, N., Neukirchen, S., Roettger, M., Nelson-Sathi, S., & Martin, W. F. (2016). The physiology and habitat of the last universal common ancestor. Nature Microbiology, 1(9). doi:10.1038/nmicrobiol.2016.116 | es_ES |
dc.description.references | Imai, A., Matsuyama, T., Hanzawa, Y., Akiyama, T., Tamaoki, M., Saji, H., … Takahashi, T. (2004). Spermidine Synthase Genes Are Essential for Survival of Arabidopsis. Plant Physiology, 135(3), 1565-1573. doi:10.1104/pp.104.041699 | es_ES |
dc.description.references | Hamasaki-Katagiri, N., Tabor, C. W., & Tabor, H. (1997). Spermidine biosynthesis in Saccharomyces cerevisiae: Polyaminerequirement of a null mutant of the SPE3 gene (spermidine synthase). Gene, 187(1), 35-43. doi:10.1016/s0378-1119(96)00660-9 | es_ES |
dc.description.references | Mandal, S., Mandal, A., Johansson, H. E., Orjalo, A. V., & Park, M. H. (2013). Depletion of cellular polyamines, spermidine and spermine, causes a total arrest in translation and growth in mammalian cells. Proceedings of the National Academy of Sciences, 110(6), 2169-2174. doi:10.1073/pnas.1219002110 | es_ES |
dc.description.references | Park, M. H., & Wolff, E. C. (2018). Hypusine, a polyamine-derived amino acid critical for eukaryotic translation. Journal of Biological Chemistry, 293(48), 18710-18718. doi:10.1074/jbc.tm118.003341 | es_ES |
dc.description.references | Park, M. H. (2006). The Post-Translational Synthesis of a Polyamine-Derived Amino Acid, Hypusine, in the Eukaryotic Translation Initiation Factor 5A (eIF5A). The Journal of Biochemistry, 139(2), 161-169. doi:10.1093/jb/mvj034 | es_ES |
dc.description.references | Chattopadhyay, M. K., Park, M. H., & Tabor, H. (2008). Hypusine modification for growth is the major function of spermidine in Saccharomyces cerevisiae polyamine auxotrophs grown in limiting spermidine. Proceedings of the National Academy of Sciences, 105(18), 6554-6559. doi:10.1073/pnas.0710970105 | es_ES |
dc.description.references | Pällmann, N., Braig, M., Sievert, H., Preukschas, M., Hermans-Borgmeyer, I., Schweizer, M., … Balabanov, S. (2015). Biological Relevance and Therapeutic Potential of the Hypusine Modification System. Journal of Biological Chemistry, 290(30), 18343-18360. doi:10.1074/jbc.m115.664490 | es_ES |
dc.description.references | Nishimura, K., Lee, S. B., Park, J. H., & Park, M. H. (2011). Essential role of eIF5A-1 and deoxyhypusine synthase in mouse embryonic development. Amino Acids, 42(2-3), 703-710. doi:10.1007/s00726-011-0986-z | es_ES |
dc.description.references | Pagnussat, G. C., Yu, H.-J., Ngo, Q. A., Rajani, S., Mayalagu, S., Johnson, C. S., … Sundaresan, V. (2005). Genetic and molecular identification of genes required for female gametophyte development and function inArabidopsis. Development, 132(3), 603-614. doi:10.1242/dev.01595 | es_ES |
dc.description.references | THOMAS, A., GOUMANS, H., AMESZ, H., BENNE, R., & VOORMA, H. O. (1979). A Comparison of the Initiation Factors of Eukaryotic Protein Synthesis from Ribosomes and from the Postribosomal Supernatant. European Journal of Biochemistry, 98(2), 329-337. doi:10.1111/j.1432-1033.1979.tb13192.x | es_ES |
dc.description.references | Cooper, H. L., Park, M. H., Folk, J. E., Safer, B., & Braverman, R. (1983). Identification of the hypusine-containing protein hy+ as translation initiation factor eIF-4D. Proceedings of the National Academy of Sciences, 80(7), 1854-1857. doi:10.1073/pnas.80.7.1854 | es_ES |
dc.description.references | Shiba, T., Mizote, H., Kaneko, T., Nakajima, T., Yasuo, K., & sano, I. (1971). Hypusine, a new amino acid occurring in bovine brain. Biochimica et Biophysica Acta (BBA) - General Subjects, 244(3), 523-531. doi:10.1016/0304-4165(71)90069-9 | es_ES |
dc.description.references | Park, M. H., Cooper, H. L., & Folk, J. E. (1981). Identification of hypusine, an unusual amino acid, in a protein from human lymphocytes and of spermidine as its biosynthetic precursor. Proceedings of the National Academy of Sciences, 78(5), 2869-2873. doi:10.1073/pnas.78.5.2869 | es_ES |
dc.description.references | Saini, P., Eyler, D. E., Green, R., & Dever, T. E. (2009). Hypusine-containing protein eIF5A promotes translation elongation. Nature, 459(7243), 118-121. doi:10.1038/nature08034 | es_ES |
dc.description.references | Schuller, A. P., Wu, C. C.-C., Dever, T. E., Buskirk, A. R., & Green, R. (2017). eIF5A Functions Globally in Translation Elongation and Termination. Molecular Cell, 66(2), 194-205.e5. doi:10.1016/j.molcel.2017.03.003 | es_ES |
dc.description.references | Gäbel, K., Schmitt, J., Schulz, S., Näther, D. J., & Soppa, J. (2013). A Comprehensive Analysis of the Importance of Translation Initiation Factors for Haloferax volcanii Applying Deletion and Conditional Depletion Mutants. PLoS ONE, 8(11), e77188. doi:10.1371/journal.pone.0077188 | es_ES |
dc.description.references | Kyrpides, N. C., & Woese, C. R. (1998). Universally conserved translation initiation factors. Proceedings of the National Academy of Sciences, 95(1), 224-228. doi:10.1073/pnas.95.1.224 | es_ES |
dc.description.references | Navarre, W. W., Zou, S. B., Roy, H., Xie, J. L., Savchenko, A., Singer, A., … Fang, F. C. (2010). PoxA, YjeK, and Elongation Factor P Coordinately Modulate Virulence and Drug Resistance in Salmonella enterica. Molecular Cell, 39(2), 209-221. doi:10.1016/j.molcel.2010.06.021 | es_ES |
dc.description.references | Lassak, J., Keilhauer, E. C., Fürst, M., Wuichet, K., Gödeke, J., Starosta, A. L., … Jung, K. (2015). Arginine-rhamnosylation as new strategy to activate translation elongation factor P. Nature Chemical Biology, 11(4), 266-270. doi:10.1038/nchembio.1751 | es_ES |
dc.description.references | Bullwinkle, T. J., Zou, S. B., Rajkovic, A., Hersch, S. J., Elgamal, S., Robinson, N., … Ibba, M. (2013). (R)-β-Lysine-modified Elongation Factor P Functions in Translation Elongation. Journal of Biological Chemistry, 288(6), 4416-4423. doi:10.1074/jbc.m112.438879 | es_ES |
dc.description.references | Balibar, C. J., Iwanowicz, D., & Dean, C. R. (2013). Elongation Factor P is Dispensable in Escherichia coli and Pseudomonas aeruginosa. Current Microbiology, 67(3), 293-299. doi:10.1007/s00284-013-0363-0 | es_ES |
dc.description.references | Blaha, G., Stanley, R. E., & Steitz, T. A. (2009). Formation of the First Peptide Bond: The Structure of EF-P Bound to the 70 S Ribosome. Science, 325(5943), 966-970. doi:10.1126/science.1175800 | es_ES |
dc.description.references | Melnikov, S., Mailliot, J., Shin, B.-S., Rigger, L., Yusupova, G., Micura, R., … Yusupov, M. (2016). Crystal Structure of Hypusine-Containing Translation Factor eIF5A Bound to a Rotated Eukaryotic Ribosome. Journal of Molecular Biology, 428(18), 3570-3576. doi:10.1016/j.jmb.2016.05.011 | es_ES |
dc.description.references | Schmidt, C., Becker, T., Heuer, A., Braunger, K., Shanmuganathan, V., Pech, M., … Beckmann, R. (2015). Structure of the hypusinylated eukaryotic translation factor eIF-5A bound to the ribosome. Nucleic Acids Research, 44(4), 1944-1951. doi:10.1093/nar/gkv1517 | es_ES |
dc.description.references | Gutierrez, E., Shin, B.-S., Woolstenhulme, C. J., Kim, J.-R., Saini, P., Buskirk, A. R., & Dever, T. E. (2013). eIF5A Promotes Translation of Polyproline Motifs. Molecular Cell, 51(1), 35-45. doi:10.1016/j.molcel.2013.04.021 | es_ES |
dc.description.references | Doerfel, L. K., Wohlgemuth, I., Kothe, C., Peske, F., Urlaub, H., & Rodnina, M. V. (2013). EF-P Is Essential for Rapid Synthesis of Proteins Containing Consecutive Proline Residues. Science, 339(6115), 85-88. doi:10.1126/science.1229017 | es_ES |
dc.description.references | Ude, S., Lassak, J., Starosta, A. L., Kraxenberger, T., Wilson, D. N., & Jung, K. (2013). Translation Elongation Factor EF-P Alleviates Ribosome Stalling at Polyproline Stretches. Science, 339(6115), 82-85. doi:10.1126/science.1228985 | es_ES |
dc.description.references | Pavlov, M. Y., Watts, R. E., Tan, Z., Cornish, V. W., Ehrenberg, M., & Forster, A. C. (2008). Slow peptide bond formation by proline and other N-alkylamino acids in translation. Proceedings of the National Academy of Sciences, 106(1), 50-54. doi:10.1073/pnas.0809211106 | es_ES |
dc.description.references | Belda-Palazón, B., Almendáriz, C., Martí, E., Carbonell, J., & Ferrando, A. (2016). Relevance of the Axis Spermidine/eIF5A for Plant Growth and Development. Frontiers in Plant Science, 7. doi:10.3389/fpls.2016.00245 | es_ES |
dc.description.references | Li, T., Belda-Palazón, B., Ferrando, A., & Alepuz, P. (2014). Fertility and Polarized Cell Growth Depends on eIF5A for Translation of Polyproline-Rich Formins in Saccharomyces cerevisiae. Genetics, 197(4), 1191-1200. doi:10.1534/genetics.114.166926 | es_ES |
dc.description.references | Duguay, J., Jamal, S., Liu, Z., Wang, T.-W., & Thompson, J. E. (2007). Leaf-specific suppression of deoxyhypusine synthase in Arabidopsis thaliana enhances growth without negative pleiotropic effects. Journal of Plant Physiology, 164(4), 408-420. doi:10.1016/j.jplph.2006.02.001 | es_ES |
dc.description.references | Feng, H., Chen, Q., Feng, J., Zhang, J., Yang, X., & Zuo, J. (2007). Functional Characterization of the Arabidopsis Eukaryotic Translation Initiation Factor 5A-2 That Plays a Crucial Role in Plant Growth and Development by Regulating Cell Division, Cell Growth, and Cell Death. Plant Physiology, 144(3), 1531-1545. doi:10.1104/pp.107.098079 | es_ES |
dc.description.references | Liu, Z., Duguay, J., Ma, F., Wang, T.-W., Tshin, R., Hopkins, M. T., … Thompson, J. E. (2008). Modulation of eIF5A1 expression alters xylem abundance in Arabidopsis thaliana. Journal of Experimental Botany, 59(4), 939-950. doi:10.1093/jxb/ern017 | es_ES |
dc.description.references | MA, F., LIU, Z., WANG, T.-W., HOPKINS, M. T., PETERSON, C. A., & THOMPSON, J. E. (2010). Arabidopsis eIF5A3 influences growth and the response to osmotic and nutrient stress. Plant, Cell & Environment, 33(10), 1682-1696. doi:10.1111/j.1365-3040.2010.02173.x | es_ES |
dc.description.references | Buskirk, A. R., & Green, R. (2017). Ribosome pausing, arrest and rescue in bacteria and eukaryotes. Philosophical Transactions of the Royal Society B: Biological Sciences, 372(1716), 20160183. doi:10.1098/rstb.2016.0183 | es_ES |
dc.description.references | Dever, T. E., Dinman, J. D., & Green, R. (2018). Translation Elongation and Recoding in Eukaryotes. Cold Spring Harbor Perspectives in Biology, 10(8), a032649. doi:10.1101/cshperspect.a032649 | es_ES |
dc.description.references | Zuk, D. (1998). A single amino acid substitution in yeast eIF-5A results in mRNA stabilization. The EMBO Journal, 17(10), 2914-2925. doi:10.1093/emboj/17.10.2914 | es_ES |
dc.description.references | Schrader, R., Young, C., Kozian, D., Hoffmann, R., & Lottspeich, F. (2006). Temperature-sensitive eIF5A Mutant Accumulates Transcripts Targeted to the Nonsense-mediated Decay Pathway. Journal of Biological Chemistry, 281(46), 35336-35346. doi:10.1074/jbc.m601460200 | es_ES |
dc.description.references | Hoque, M., Park, J. Y., Chang, Y., Luchessi, A. D., Cambiaghi, T. D., Shamanna, R., … Mathews, M. B. (2017). Regulation of gene expression by translation factor eIF5A: Hypusine-modified eIF5A enhances nonsense-mediated mRNA decay in human cells. Translation, 5(2), e1366294. doi:10.1080/21690731.2017.1366294 | es_ES |
dc.description.references | Li, C. H., Ohn, T., Ivanov, P., Tisdale, S., & Anderson, P. (2010). eIF5A Promotes Translation Elongation, Polysome Disassembly and Stress Granule Assembly. PLoS ONE, 5(4), e9942. doi:10.1371/journal.pone.0009942 | es_ES |
dc.description.references | Miller-Fleming, L., Olin-Sandoval, V., Campbell, K., & Ralser, M. (2015). Remaining Mysteries of Molecular Biology: The Role of Polyamines in the Cell. Journal of Molecular Biology, 427(21), 3389-3406. doi:10.1016/j.jmb.2015.06.020 | es_ES |