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


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2011-10

AUTHORS

Hervé Roy, S Betty Zou, Tammy J Bullwinkle, Benjamin S Wolfe, Marla S Gilreath, Craig J Forsyth, William W Navarre, Michael Ibba

ABSTRACT

The lysyl-tRNA synthetase paralog PoxA modifies elongation factor P (EF-P) with α-lysine at low efficiency. Cell-free extracts containing non-α-lysine substrates of PoxA modified EF-P with a change in mass consistent with addition of 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. More... »

PAGES

667

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nchembio.632

DOI

http://dx.doi.org/10.1038/nchembio.632

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1021807001

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/21841797


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