The duality of LysU, a catalyst for both Ap4A and Ap 3A formation

FEBS Journal

Volumn 273, Issue 15, 2006, Pages 3534-3544

  Wright, Michael ^a   Boonyalai, Nonlawat ^a   Tanner, Julian A ^a   Hindley, Alison D ^a   Miller, Andrew D ^a  

^a IMPERIAL COLLEGE LONDON   (United Kingdom)

Author keywords

Ap3A; Ap4A; Dinucleoside polyphosphates; Heat shock response; LysU

Indexed keywords

ADENOSINE PHOSPHATE; DIADENOSINE TETRAPHOSPHATE; DIADENOSINE TRIPHOSPHATE; ENZYME LYSU; LYSINE TRANSFER RNA LIGASE; PHOSPHATE; SYNTHETASE; UNCLASSIFIED DRUG;

ARTICLE; CATALYST; EUKARYOTIC CELL; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; ION EXCHANGE CHROMATOGRAPHY; MOLECULAR MECHANICS; PHOSPHORYLATION; PRIORITY JOURNAL; PROTEIN FUNCTION;

BLOTTING, WESTERN; CATALYSIS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CHROMATOGRAPHY, ION EXCHANGE; DINUCLEOSIDE PHOSPHATES; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; LYSINE-TRNA LIGASE; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PHOSPHORYLATION;

ESCHERICHIA COLI; EUKARYOTA; PROKARYOTA;

EID: 33746162021     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2006.05361.x     Document Type: Article

References (38)

1. Cusack S, Hartlein M & Leberman R (1991) Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases. Nucleic Acids Res 19, 3489-3498.
2. Onesti S, Miller AD & Brick P (1995) The crystal structure of the lysyl-tRNA synthetase (LysU) from Escherichia coli. Structure 3, 163-176.
3. Ito K, Oshima T, Mizuno T & Nakamura Y (1994) Regulation of lysyl-tRNA synthetase expression by histone-like protein H-NS of Escherichia coli. J Bacteriol 176, 7383-7386.
4. Brevet A, Chen J, Leveque F, Blanquet S & Plateau P (1995) Comparison of the enzymatic properties of the two Escherichia coli lysyl-tRNA synthetase species. J Biol Chem 270, 14439-14444.
5. Charlier J & Sanchez R (1987) Lysyl-tRNA synthetase from Escherichia coli K12. Chromatographic heterogeneity and the lysU-gene product. Biochem J 248, 43-51.
6. Brevet A, Chen J, Leveque F, Plateau P & Blanquet S (1989) In vivo synthesis of adenylylated bis (5′-nucleosidyl) tetraphosphates (Ap4N) by Escherichia coli aminoacyl-tRNA synthetases. Proc Natl Acad Sci USA 86, 8275-8279.
7. Theoclitou ME & Miller AD (1994) Enhancement of molecular ion intensity of synthetic analogues of diadenosine 5′,5″-P1,P4- tetraphosphate (Ap4A) in negative-ion mode fast atom bombardment mass spectrometry. Anal Biochem 218, 235-237.
8. Zamecnik PC, Stephenson ML, Janeway CM & Randerath K (1966) Enzymatic synthesis of diadenosine tetraphosphate and diadenosine triphosphate with a purified lysyl-sRNA synthetase. Biochem Biophys Res Commun 24, 91-97.
9. Theoclitou ME, El-Thaher TSH & Miller AD (1994) Enzymatic synthesis of diadenosine 5′,5‴-P1,P4-tetraphosphate (Ap4A) analogues by stress protein LysU. J Chem Soc Chem Commun 1994, 659-661.
10. Wright M, Tanner JA & Miller AD (2003) Quantitative single-step purification of dinucleoside polyphosphates. Anal Biochem 316, 123-138.
11. Wright M & Miller AD (2004) Synthesis of novel fluorescent-labelled dinucleoside polyphosphates. Bioorg Med Chem Lett 14, 2813-2816.
12. Wright M & Miller AD (2006) Novel fluorescent labelled affinity probes for diadenosine-5′,5‴-P1,P4-tetraphosphate (Ap4A) binding studies. Bioorg Med Chem Lett 16, 943-948.
13. Randerath K, Janeway CM, Stephenson ML & Zamecnik PC (1966) Isolation and characterization of dinucleoside tetra- and tri-phosphates formed in the presence of lysyl-sRNA synthetase. Biochem Biophys Res Commun 24, 98-105.
14. 4A) analogues by LysU. J Chem Soc Perkin Trans 1, 2009-2019.
15. Plateau P, Mayaux JF & Blanquet S (1981) Zinc (II)-dependent synthesis of diadenosine 5′,5″-P(1),P(4)-tetraphosphate by Escherichia coli and yeast phenylalanyl transfer ribonucleic acid synthetases. Biochemistry 20, 4654-4662.
16. McLennan AG, Taylor GE, Prescott M & Blackburn GM (1989) Recognition of beta beta′-substituted and alpha beta,alpha′beta′- disubstituted phosphonate analogues of bis(5′-adenosyl) tetraphosphate by the bis(5′-nucleosidyl)-tetraphosphate pyrophosphohydrolases from Artemia embryos and Escherichia coli. Biochemistry 28, 3868-3875.
17. Led JJ, Switon WK & Jensen KF (1983) Phosphorolytic activity of Escherichia coli glycyl-tRNA synthetase towards its cognate aminoacyl adenylate detected by 31P-NMR spectroscopy and thin-layer chromatography. Eur J Biochem 136, 469-479.
18. Hughes SJ, Tanner JA, Hindley AD, Miller AD & Gould IR (2003) Functional asymmetry in the lysyl-tRNA synthetase explored by molecular dynamics, free energy calculations and experiment. BMC Struct Biol 3, 5-25.
19. Leveque F, Plateau P, Dessen P & Blanquet S (1990) Homology of lysS and lysU, the two Escherichia coli genes encoding distinct lysyl-tRNA synthetase species. Nucleic Acids Res 18, 305-312.
20. Gorbunoff MJ (1984) The interaction of proteins with hydroxyapatite. I. Role of protein charge and structure. Anal Biochem 136, 425-445.
21. Cogan EB, Birrell GB & Griffith OH (1999) A robotics-based automated assay for inorganic and organic phosphates. Anal Biochem 271, 29-35.
22. Vinogradova RP, Kucherenko NE, Verkhogliad IN & Mirutenko NV (1982) Phosphorylation of lysyl tRNA synthetase from the liver of rats exposed to x-rays. Radiobiologiia 22, 446-449.
23. Vinogradova RP & Mirutenko NV (1979) Phosphorylation of aminoacyl-tRNA synthetase preparations of rat liver tissues in vivo and in vitro. Ukr Biokhim Zh 51, 596-599.
24. Pendergast AM, Venema RC & Traugh JA (1987) Regulation of phosphorylation of aminoacyl-tRNA synthetases in the high molecular weight core complex in reticulocytes. J Biol Chem 262, 5939-5942.
25. Dang CV & Traugh JA (1989) Phosphorylation of threonyl- and seryl-tRNA synthetase by cAMP-dependent protein kinase. A possible role in the regulation of P1,P4-bis (5′-adenosyl)-tetraphosphate (Ap4A) synthesis. J Biol Chem 264, 5861-5865.
26. Tanner JA, Abowath A & Miller AD (2002) Isothermal titration calorimetry reveals a zinc ion as an atomic switch in the diadenosine polyphosphates. J Biol Chem 277, 3073-3078.
27. Plateau P & Blanquet S (1982) Zinc-dependent synthesis of various dinucleoside 5′,5‴-P1,P3-Tri- or 5″,5‴-P1,P4- tetraphosphates by Escherichia coli lysyl-tRNA synthetase. Biochemistry 21, 5273-5279.
28. Lloyd AJ, Thomann HU, Ibba M & Soll D (1995) A broadly applicable continuous spectrophotometric assay for measuring aminoacyl-tRNA synthetase activity. Nucleic Acids Res 23, 2886-2892.
29. Webb MR (1992) A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems. Proc Natl Acad Sci USA 89, 4884-4887.
30. Vartanian A, Prudovsky I, Suzuki H, Dal Pra I & Kisselev L (1997) Opposite effects of cell differentiation and apoptosis on Ap3A/Ap4A ratio in human cell cultures. FEBS Lett 415, 160-162.
31. Vartanian A, Alexandrov I, Prudowski I, McLennan A & Kisselev L (1999) Ap4A induces apoptosis in human cultured cells. FEBS Lett 456, 175-180.
32. Jankowski J, Jankowski V, Laufer U, van der Giet M, Henning L, Tepel M, Zidek W & Schluter H (2003) Identification and quantification of diadenosine polyphosphate concentrations in human plasma. Arterioscler Thromb Vasc Biol 23, 1231-1238.
33. Luthje J, Baringer J & Ogilvie A (1985) Effects of diadenosine triphosphate (Ap3A) and diadenosine tetraphosphate (Ap4A) on platelet aggregation in unfractionated human blood. Blut 51, 405-413.
34. Pintor J, Peral A, Pelaez T, Martin S & Hoyle CH (2003) Presence of diadenosine polyphosphates in the aqueous humor: their effect on intraocular pressure. J Pharmacol Exp Ther 304, 342-348.
35. Kisselev LL, Justesen J, Wolfson AD & Frolova LY (1998) Diadenosine oligophosphates (Ap (n) A), a novel class of signalling molecules? FEBS Lett 427, 157-163.
36. Ogilvie A & Jakob P (1983) Diadenosine 5′,5″-P1,P3- triphosphate in eukaryotic cells: identification and quantitation. Anal Biochem 134, 382-392.
37. Gill SC & von Hippel PH (1985) Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 182, 316-326.
38. Buss JE & Stull JT (1983) Measurement of chemical phosphate in proteins. Methods Enzymol 99, 7-14.