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Pregledni rad
https://doi.org/10.5562/cca2908

Seryl-tRNA Synthetases in Translation and Beyond

Marko Močibob ; Department of Chemistry, Faculty of Science, University of Zagreb, Horvatovac 102a, HR-10000 Zagreb, Croatia
Jasmina Rokov-Plavec ; Department of Chemistry, Faculty of Science, University of Zagreb, Horvatovac 102a, HR-10000 Zagreb, Croatia
Vlatka Godinić-Mikulčić ; Department of Chemistry, Faculty of Science, University of Zagreb, Horvatovac 102a, HR-10000 Zagreb, Croatia
Ita Gruić-Sovulj ; Department of Chemistry, Faculty of Science, University of Zagreb, Horvatovac 102a, HR-10000 Zagreb, Croatia

Puni tekst: engleski, pdf (2 MB) str. 261-276 preuzimanja: 928* citiraj
APA 6th Edition
Močibob, M., Rokov-Plavec, J., Godinić-Mikulčić, V. i Gruić-Sovulj, I. (2016). Seryl-tRNA Synthetases in Translation and Beyond. Croatica Chemica Acta, 89 (2), 261-276. https://doi.org/10.5562/cca2908
MLA 8th Edition
Močibob, Marko, et al. "Seryl-tRNA Synthetases in Translation and Beyond." Croatica Chemica Acta, vol. 89, br. 2, 2016, str. 261-276. https://doi.org/10.5562/cca2908. Citirano 07.03.2021.
Chicago 17th Edition
Močibob, Marko, Jasmina Rokov-Plavec, Vlatka Godinić-Mikulčić i Ita Gruić-Sovulj. "Seryl-tRNA Synthetases in Translation and Beyond." Croatica Chemica Acta 89, br. 2 (2016): 261-276. https://doi.org/10.5562/cca2908
Harvard
Močibob, M., et al. (2016). 'Seryl-tRNA Synthetases in Translation and Beyond', Croatica Chemica Acta, 89(2), str. 261-276. https://doi.org/10.5562/cca2908
Vancouver
Močibob M, Rokov-Plavec J, Godinić-Mikulčić V, Gruić-Sovulj I. Seryl-tRNA Synthetases in Translation and Beyond. Croatica Chemica Acta [Internet]. 2016 [pristupljeno 07.03.2021.];89(2):261-276. https://doi.org/10.5562/cca2908
IEEE
M. Močibob, J. Rokov-Plavec, V. Godinić-Mikulčić i I. Gruić-Sovulj, "Seryl-tRNA Synthetases in Translation and Beyond", Croatica Chemica Acta, vol.89, br. 2, str. 261-276, 2016. [Online]. https://doi.org/10.5562/cca2908

Sažetak
For a long time seryl-tRNA synthetases (SerRSs) stood as an archetypal, canonical aminoacyl-tRNA synthetases (aaRS), exhibiting only basic tRNA aminoacylation activity and with no moonlighting functions beyond protein biosynthesis. The picture has changed substantially in recent years after the discovery that SerRSs play an important role in antibiotic production and resistance and act as a regulatory factor in vascular development, as well as after the discovery of mitochondrial morphogenesis factor homologous to SerRS in insects. In this review we summarize the recent research results from our laboratory, which advance the understanding of seryl-tRNA synthetases and further paint the dynamic picture of unexpected SerRS activities. SerRS from archaeon Methanothermobacter thermautotrophicus was shown to interact with the large ribosomal subunit and it was postulated to contribute to a more efficient translation by the"tRNA channeling" hypothesis. Discovery of the atypical SerRS in a small number of methanogenic archaea led to the discovery of a new family of enzymes in numerous bacteria - amino acid:[carrier protein] ligases (aa:CP ligases). These SerRS homologues resigned tRNA aminoacylation activity, and instead adopted carrier proteins as the acceptors of activated amino acids. The crystal structure of the aa:CP ligase complex with the carrier protein revealed that the interactions between two macromolecules are incomparable to tRNA binding by the aaRS and consequently represent a true evolutionary invention. Kinetic investigations of SerRSs and the accuracy of amino acid selection revealed that SerRSs possess pre-transfer proofreading activity, challenging the widely accepted presumption that hydrolytic proofreading activity must reside in an additional, separate editing domain, not present in SerRSs. Finally, the plant tRNA serylation system is discussed, which is particularly interesting due to the fact that protein biosynthesis takes place in three cellular compartments: cytosol, mitochondria and chloroplasts. Plant cytosolic SerRSs showed broad tRNASer specificity and flexibility, unlike SerRSs from other organisms. High fidelity of SerRS dually targeted to mitochondria and chloroplasts indicated its importance in plant organellar quality control.

Creative Commons License This work is licensed under a Creative Commons Attribution 4.0 International License.

Ključne riječi
seryl-tRNA synthetase; editing; proofreading; protein complexes; amino acid:[carrier protein] ligase; carrier protein; ribosome; plant

Projekti
EC / FP7 / 315997 / INTEGRA-LIFE - Integrating research in molecular life sciences at the University of Zagreb

Hrčak ID: 168001

URI
https://hrcak.srce.hr/168001

Posjeta: 1.225 *