Potassium functionally replaces the second lysine of the KMSKS signature sequence in human tyrosyl-tRNA synthetase.

The Journal of Biological Chemistry
Joseph Austin, E A First

Abstract

Unlike their bacterial homologues, a number of eukaryotic tyrosyl-tRNA synthetases require potassium to catalyze the aminoacylation reaction. In addition, the second lysine in the class I-specific KMSKS signature motif is absent from all known eukaryotic tyrosyl-tRNA synthetase sequences, except those of higher plants. This lysine, which is the most highly conserved residue in the class I aminoacyl-tRNA synthetase family, has been shown to interact with the pyrophosphate moiety of the ATP substrate in the Bacillus stearothermophilus tyrosyl-tRNA synthetase. Equilibrium dialysis and pre-steady-state kinetic analyses were used to determine the role that potassium plays in the tyrosine activation reaction in the human tyrosyl-tRNA synthetase and whether it can be replaced by any of the other alkali metals. Kinetic analyses indicate that potassium interacts with the pyrophosphate moiety of ATP, stabilizing the E.Tyr.ATP and E.[Tyr-ATP] complexes by 2.3 and 4.3 kcal/mol, respectively. Potassium also appears to stabilize the asymmetric conformation of the human tyrosyl-tRNA synthetase dimer by 0.7 kcal/mol. Rubidium is the only other alkali metal that can replace potassium in catalyzing tyrosine activation, although the forward rate ...Continue Reading

References

Nov 1, 1992·The Journal of Antimicrobial Chemotherapy·T H FarmerS W Elson
Feb 1, 1989·Antimicrobial Agents and Chemotherapy·J O CapobiancoR C Goldman
Mar 27, 1972·European Journal of Biochemistry·H BeikirchF Cramer
May 24, 1974·Nature·G L KochB S Hartley
May 30, 1997·The Journal of Biological Chemistry·T A KleemanE A First
Aug 1, 1997·Current Opinion in Chemical Biology·K Bush
Feb 24, 2001·The Journal of Antibiotics·A L StefanskaS R Warr
Feb 22, 2002·The Journal of Biological Chemistry·Joseph Austin, Eric A First

❮ Previous
Next ❯

Citations

Dec 17, 2009·Nature Structural & Molecular Biology·Quansheng ZhouXiang-Lei Yang
Apr 24, 2009·Journal of Biochemistry·Shunsuke KamijoKenichi Wakabayashi
Apr 12, 2014·Journal of Structural and Functional Genomics·Manish Datt, Amit Sharma
Apr 28, 2007·Expert Opinion on Investigational Drugs·Urs A OchsnerNebojsa Janjic
Jan 25, 2005·Journal of Molecular Biology·Takatsugu KobayashiShigeyuki Yokoyama
Dec 6, 2005·Journal of Molecular Biology·Mitsuo KurataniShigeyuki Yokoyama
May 3, 2016·Environmental Science & Technology·Zhen WangSen Miao
Oct 30, 2016·Journal of Biomolecular Structure & Dynamics·Vladyslav O KravchukAlexander I Kornelyuk
Mar 21, 2019·American Journal of Physiology. Lung Cellular and Molecular Physiology·Luciano AmarelleJacob I Sznajder

❮ Previous
Next ❯

Related Concepts

Related Feeds

Antifungals (ASM)

An antifungal, also known as an antimycotic medication, is a pharmaceutical fungicide or fungistatic used to treat and prevent mycosis such as athlete's foot, ringworm, candidiasis, cryptococcal meningitis, and others. Discover the latest research on antifungals here.

ASBMB Publications

The American Society for Biochemistry and Molecular Biology (ASBMB) includes the Journal of Biological Chemistry, Molecular & Cellular Proteomics, and the Journal of Lipid Research. Discover the latest research from ASBMB here.

Antifungals

An antifungal, also known as an antimycotic medication, is a pharmaceutical fungicide or fungistatic used to treat and prevent mycosis such as athlete's foot, ringworm, candidiasis, cryptococcal meningitis, and others. Discover the latest research on antifungals here.