The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine

The lysyl-tRNA synthetase paralog PoxA modifies elongation factor P (EF-P) with α-lysine at low efficiency. Cell-free extracts contained non-α-lysine substrates of PoxA that modified EF-P by a change in mass consistent with β–lysine, a substrate also predicted by genomic analyses. EF-P was efficient...

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Autores principales: Roy, Hervé, Zou, S. Betty, Bullwinkle, Tammy J., Wolfe, Benjamin S., Gilreath, Marla S., Forsyth, Craig J., Navarre, William W., Ibba, Michael
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2011
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3177975/
https://www.ncbi.nlm.nih.gov/pubmed/21841797
http://dx.doi.org/10.1038/nchembio.632
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author Roy, Hervé
Zou, S. Betty
Bullwinkle, Tammy J.
Wolfe, Benjamin S.
Gilreath, Marla S.
Forsyth, Craig J.
Navarre, William W.
Ibba, Michael
author_facet Roy, Hervé
Zou, S. Betty
Bullwinkle, Tammy J.
Wolfe, Benjamin S.
Gilreath, Marla S.
Forsyth, Craig J.
Navarre, William W.
Ibba, Michael
author_sort Roy, Hervé
collection PubMed
description The lysyl-tRNA synthetase paralog PoxA modifies elongation factor P (EF-P) with α-lysine at low efficiency. Cell-free extracts contained non-α-lysine substrates of PoxA that modified EF-P by a change in mass consistent with β–lysine, a substrate also predicted by genomic analyses. EF-P was efficiently, functionally, modified with (R)-β-lysine but not (S)-β-lysine or genetically encoded α-amino acids, indicating that PoxA has evolved an activity orthogonal to that of the canonical aminoacyl-tRNA synthetases.
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spelling pubmed-31779752012-04-01 The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine Roy, Hervé Zou, S. Betty Bullwinkle, Tammy J. Wolfe, Benjamin S. Gilreath, Marla S. Forsyth, Craig J. Navarre, William W. Ibba, Michael Nat Chem Biol Article The lysyl-tRNA synthetase paralog PoxA modifies elongation factor P (EF-P) with α-lysine at low efficiency. Cell-free extracts contained non-α-lysine substrates of PoxA that modified EF-P by a change in mass consistent with β–lysine, a substrate also predicted by genomic analyses. EF-P was efficiently, functionally, modified with (R)-β-lysine but not (S)-β-lysine or genetically encoded α-amino acids, indicating that PoxA has evolved an activity orthogonal to that of the canonical aminoacyl-tRNA synthetases. 2011-08-14 /pmc/articles/PMC3177975/ /pubmed/21841797 http://dx.doi.org/10.1038/nchembio.632 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Roy, Hervé
Zou, S. Betty
Bullwinkle, Tammy J.
Wolfe, Benjamin S.
Gilreath, Marla S.
Forsyth, Craig J.
Navarre, William W.
Ibba, Michael
The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine
title The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine
title_full The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine
title_fullStr The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine
title_full_unstemmed The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine
title_short The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine
title_sort trna synthetase paralog poxa modifies elongation factor-p with (r)-β-lysine
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3177975/
https://www.ncbi.nlm.nih.gov/pubmed/21841797
http://dx.doi.org/10.1038/nchembio.632
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