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Abstract:

Regulation of protein synthesis contributes to maintenance of homeostasis and adaptation to environmental changes. mRNA translation is controlled at various levels including initiation, elongation and termination, through post-transcriptional/translational modifications of components of the protein synthesis machinery. Recently, protein and RNA hydroxylation have emerged as important enzymatic modifications of tRNAs, elongation and termination factors, as well as ribosomal proteins. These modifications enable a correct STOP codon recognition, ensuring translational fidelity. Recent studies are starting to show that STOP codon read-through is related to the ability of the cell to cope with different types of stress, such as oxidative and chemical insults, while correlations between defects in hydroxylation of protein synthesis components and STOP codon read-through are beginning to emerge. In this review we will discuss our current knowledge of protein synthesis regulation through hydroxylation of components of the translation machinery, with special focus on STOP codon recognition. We speculate on the possibility that programmed STOP codon read-through, modulated by hydroxylation of components of the protein synthesis machinery, is part of a concerted cellular response to stress. © 2016 Springer International Publishing.

Registro:

Documento: Artículo
Título:Hydroxylation and translational adaptation to stress: Some answers lie beyond the STOP codon
Autor:Katz, M.J.; Gándara, L.; De Lella Ezcurra, A.L.; Wappner, P.
Filiación:Instituto Leloir, Buenos Aires, Argentina
Departamento de Fisiología, Biología Molecular, y Celular, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina
Palabras clave:Dioxygenases; Post-translational modifications; Protein synthesis; Translational fidelity; elongation factor; ribosome protein; transfer RNA; dioxygenase; ribosome protein; stop codon; transfer RNA; cell stress; codon; human; hydroxylation; nonhuman; protein synthesis; Review; stop codon; stop codon read through; transcription elongation; transcription termination; translation regulation; bacterium; genetics; hydroxylation; metabolism; oxidative stress; protein processing; stop codon; Bacteria; Codon, Terminator; Dioxygenases; Humans; Hydroxylation; Oxidative Stress; Protein Processing, Post-Translational; Ribosomal Proteins; RNA, Transfer
Año:2016
Volumen:73
Número:9
Página de inicio:1881
Página de fin:1893
DOI: http://dx.doi.org/10.1007/s00018-016-2160-y
Título revista:Cellular and Molecular Life Sciences
Título revista abreviado:Cell. Mol. Life Sci.
ISSN:1420682X
CODEN:CMLSF
CAS:transfer RNA, 9014-25-9; dioxygenase, 37292-90-3; Codon, Terminator; Dioxygenases; Ribosomal Proteins; RNA, Transfer
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_1420682X_v73_n9_p1881_Katz

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Citas:

---------- APA ----------
Katz, M.J., Gándara, L., De Lella Ezcurra, A.L. & Wappner, P. (2016) . Hydroxylation and translational adaptation to stress: Some answers lie beyond the STOP codon. Cellular and Molecular Life Sciences, 73(9), 1881-1893.
http://dx.doi.org/10.1007/s00018-016-2160-y
---------- CHICAGO ----------
Katz, M.J., Gándara, L., De Lella Ezcurra, A.L., Wappner, P. "Hydroxylation and translational adaptation to stress: Some answers lie beyond the STOP codon" . Cellular and Molecular Life Sciences 73, no. 9 (2016) : 1881-1893.
http://dx.doi.org/10.1007/s00018-016-2160-y
---------- MLA ----------
Katz, M.J., Gándara, L., De Lella Ezcurra, A.L., Wappner, P. "Hydroxylation and translational adaptation to stress: Some answers lie beyond the STOP codon" . Cellular and Molecular Life Sciences, vol. 73, no. 9, 2016, pp. 1881-1893.
http://dx.doi.org/10.1007/s00018-016-2160-y
---------- VANCOUVER ----------
Katz, M.J., Gándara, L., De Lella Ezcurra, A.L., Wappner, P. Hydroxylation and translational adaptation to stress: Some answers lie beyond the STOP codon. Cell. Mol. Life Sci. 2016;73(9):1881-1893.
http://dx.doi.org/10.1007/s00018-016-2160-y