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2002 | 49 | 4 |

Tytuł artykułu

The effect of vanadate on Pichia pastoris growth, protein kinase A activity and ribosomal protein phosphorylation

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
It was found that wild type yeast Pichia pastoris can tolerate vanadate concentration as high as 25 mM in the growth medium. Moreover, four vanadate-resistant P. pastoris strains designated JC100/1, JC100/3, JC100/9 and JC100/15 exhibiting tol­erance up to 150 mM vanadate were selected. Growth of P. pastoris was correlated with vanadate to vanadyl reduction and its accumulation in the growth medium. In two selected strains, JC100/9 and JC100/15, protein kinase A activity was much higher in comparison to the wild type strain even without vanadate addition to the growth medium. Moreover, in the presence of vanadate, protein kinase A activity was significantly increased in the wild type and the vanadate-resistant JC100/1 and JC100/3 strains. It was also found that phosphorylation of a 40 kDa protein associ­ated with ribosomes occured in all vanadate-resistant strains from the logarithmic, while in the wild type strain from the stationary growth phase. From the presented re­sults it can be concluded that a protein kinase A signalling pathway(s) might be in­volved in the mechanism of P. pastoris vanadate resistance. The results also indicate a possible role of the 40 kDa protein in protection of P. pastoris against vanadate toxicity.

Wydawca

-

Rocznik

Tom

49

Numer

4

Opis fizyczny

p.959-968,fig.

Twórcy

autor
  • Maria Curie-Sklodowska University, Akademicka 19, 20-033 Lublin, Poland
autor

Bibliografia

  • Bisconti L, Pepi M, Mangani S, Baldi F. (1997) Reduction of vanadate to vanadyl by a strain of Saccharomyces cerevisiae. BioMetals.; 10: 239-46.
  • Bowman BJ, Allen KE, Slayman CW. (1983) Vanadate-resistant mutants of Neurospora crassa are deficient in a high- affinity phosphate transport system. J Bacteriol.; 153: 292-6.
  • Bradford MM. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein — dye binding. AnalBiochem.; 72: 248-54.
  • Carlson RMK. (1975) Nuclear magnetic resonance spectrum of living tunicate blood cells and the structure of the native vanadium chromogen. Proc Natl Acad Sci USA.; 72: 2217-21.
  • Catalan RE, Martinez AM, Aragones MD. (1980) Effects of vanadate on the cyclic AMP-protein kinase system in rat liver. Biochem Biophys Res Commun.; 96: 672-7.
  • Chasteen ND. (1984) The biochemistry of vanadium. Struct Bonding.; 53: 104-38.
  • Cytrynska M, Frajnt M, Jakubowicz T. (2001) Saccharomyces cerevisiae pyruvate kinase Pyk1 is PKA phosphorylation substrate in vitro. FEMSMicrobiol Lett.; 203: 223-7.
  • Cytrynska M, Wojda I, Frajnt M, Jakubowicz T. (1999) PKA from Saccharomyces cerevisiae can be activated by cyclic AMP and cyclic GMP. Can J Microbiol.; 45: 31-7.
  • Goodno CC. (1979) Inhibition of myosin ATPase by vanadate ion. Proc Natl Acad Sci USA.; 76: 2620-4.
  • Gordon JA. (1991) Use of vanadate as protein- phosphotyrosine phosphatase inhibitor. Methods Enzymol.; 201: 477-82.
  • Hackbarth I, Schmitz W, Scholz H, Wetzel E, Erdmann E, Krawietz W, Philipp G. (1980) Stimulatory effect of vanadate on cyclic AMP levels in cat papillary muscle. Biochem Pharmacol.; 29: 1429-22.
  • Juan-Vidales F, Saenz-Roblez MT, Ballesta JPG. (1984) Acidic proteins of the large ribosomal subunit in Saccharomyces cerevisiae. Effect of phosphorylation. Biochemistry.; 23: 390-6.
  • Kanik-Ennulat C, Montalvo E, Neff N. (1995) Sodium orthovanadate-resistant mutants of Saccharomyces cerevisiae show defects in Golgi mediated protein glycosylation, sporulation and detergent resistance. Genetics.; 140: 933-43.
  • Karlish SJD, Beauge LA, Glynn IM. (1979) Vanadate inhibits (Na++K+)ATPase by blocking a conformational change of the unphosphorylated form. Nature.; 282: 333-5.
  • Laemmli UK. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature.; 227: 680-5.
  • Lew DJ, Sanford MS. (1991) Characterization of constitutive exocytosis in the yeast Saccharomyces cerevisiae. JMembr Biol.; 123: 261-8.
  • Lindquist RN, Lynn JL, Lienhard GE. (1973) Possible transition-state analogs for ribonuclease. The complexes of uridine with oxovanadium (IV) ion and vanadium (V) ion. J Am Chem Soc.; 95: 8762-8.
  • Mahanty SK, Khaware R, Ansari S, Gupta P, Prasad R. (1991) Vanadate-resistant mutants of Candida albicans show alterations in phosphate uptake. FEMS Microbiol Lett.; 68: 163-6.
  • Mannazzu I, Guerra E, Strabbioli R, Masia A, Maestrale GB, Zoroddu MA, Fatichenti F. (1997) Vanadium affects vacuolation and phosphate metabolism in Hansenula polymorpha. FEMS Microbiol Lett.; 147: 23-8.
  • Morinville A, Maysinger D, Shaver A. (1998) From Vanadis to Atropos: vanadium compounds as pharmacological tools in cell death signalling. Trends Pharmacol Sci.; 19: 452-60.
  • Pandey SK, Chiasson JL, Srivastava AK. (1995) Vanadium salts stimulate mitogen-activated protein (MAP) kinases and ribosomal S6 kinases. Mol Cell Biochem.; 153: 69-78.
  • Rehder D. (1992) Structure and function of vanadium compounds in living organisms. BioMetals.; 5: 3-12.
  • Van der Zeijst BAM, Kool AJ, Bloemers HPJ. (1972) Isolation of active ribosomal subunits from yeast. Eur J Biochem.; 30: 15-25.
  • Wach A, Graber P. (1991) The plasma membrane H+-ATPase from yeast. Effects of pH, vanadate and erythrosine B on ATP hydrolysis and ATP binding. Eur J Biochem.; 201: 91-7.
  • Willsky GR, White DA, McCabe BC. (1984) Metabolism of added orthovanadate to vanadyl and high-molecular weight vanadates by Saccharomyces cerevisiae. J Biol Chem.; 259: 13273-81.
  • Wojda I, Cytrynska M, Frajnt M, Jakubowicz T. (1999) Phosphorylation of yeast ribosomal proteins by CKI and CKII in the presence of heparin. Acta Biochim Polon.; 46: 211-5.
  • Zoroddu MA, Fruianu M, Dallocchio R, Masia A. (1996) Electron paramagnetic resonance studies and effects of vanadium in Saccharomyces cerevisiae. BioMetals.; 9: 91-7.

Typ dokumentu

Bibliografia

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