Format

Send to

Choose Destination
Nat Chem Biol. 2011 Aug 14;7(10):667-9. doi: 10.1038/nchembio.632.

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

Author information

1
Department of Microbiology, Center for RNA Biology, Ohio State University, Columbus, Ohio, USA.

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.

PMID:
21841797
PMCID:
PMC3177975
DOI:
10.1038/nchembio.632
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Nature Publishing Group Icon for PubMed Central
Loading ...
Support Center