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

ABSTRACT: The lysyl-tRNA synthetase paralog PoxA modifies elongation factor P (EF-P) with ?-lysine at low efficiency. Cell-free extracts containing non-?-lysine substrates of PoxA modified EF-P with a change in mass consistent with addition of ?-lysine, a substrate also predicted by genomic analyses. EF-P was efficiently functionally modified with (R)-?-lysine but not (S)-?-lysine or genetically encoded ?-amino acids, indicating that PoxA has evolved an activity orthogonal to that of the canonical aminoacyl-tRNA synthetases.

SUBMITTER: Roy H

PROVIDER: S-EPMC3177975 | biostudies-literature | 2011 Aug

REPOSITORIES: biostudies-literature

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

Roy Hervé H Zou S Betty SB Bullwinkle Tammy J TJ Wolfe Benjamin S BS Gilreath Marla S MS Forsyth Craig J CJ Navarre William W WW Ibba Michael M

Nature chemical biology 20110814 10

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 aminoac ...[more]

PMID: 21841797

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