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

TY - JOUR

T1 - The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-ß-lysine

AU - Roy, Hervé

AU - Zou, S Betty

AU - Bullwinkle, Tammy J

AU - Wolfe, Benjamin S

AU - Gilreath, Marla S

AU - Forsyth, Craig J

AU - Navarre, William W

AU - Ibba, Michael

PY - 2011/10

Y1 - 2011/10

N2 - 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.

AB - 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.

KW - Lysine

KW - Lysine-tRNA Ligase

KW - Models, Molecular

KW - Molecular Structure

KW - Peptide Elongation Factors

KW - Stereoisomerism

U2 - 10.1038/nchembio.632

DO - 10.1038/nchembio.632

M3 - Journal article

C2 - 21841797

SN - 1552-4450

VL - 7

SP - 667

EP - 669

JO - Nature Chemical Biology

JF - Nature Chemical Biology

IS - 10

ER -