The Journal of Nutritional Biochemistry
Volume 16, Issue 7 , Pages 438-440 , July 2005

Effects of biotin on growth and protein biotinylation in Saccharomyces cerevisiae

  • Victoriano Pérez-Vázquez

      Affiliations

    • Unidad de Genética de la Nutrición, Instituto de Investigaciones Biomédicas, UNAM, Mexico, D.F. 04530, Mexico
    • Instituto Nacional de Pediatría, Av. del IMAN No. 1, 4o. piso, Mexico, D.F. 04530, Mexico
  • ,
  • Salvador Uribe

      Affiliations

    • Instituto de Fisiología Celular, UNAM, Apartado Postal 70-600, Mexico, D.F. 04510, Mexico
  • ,
  • Antonio Velázquez-Arellano

      Affiliations

    • Unidad de Genética de la Nutrición, Instituto de Investigaciones Biomédicas, UNAM, Mexico, D.F. 04530, Mexico
    • Instituto Nacional de Pediatría, Av. del IMAN No. 1, 4o. piso, Mexico, D.F. 04530, Mexico
    • Corresponding Author InformationCorresponding author. Torre de Investigación, INP, Av. del IMAN No. 1, 4o. piso, Mexico, D.F. 04530, Mexico. Tel.: +52 55 5606 3489; fax: +52 55 5606 3489.

Received 30 March 2005 ,Revised 30 March 2005 ,Accepted 30 March 2005.

References 

  1. Wolf B. Disorders of biotin metabolism. In:  Scriver C,  Beaudet AL,  Sly WS,  Vogelstein B,  Kinzler KW,  Valle D, et al. editor. The metabolic and molecular bases of inherited disease. 8th ed.. New York: McGraw-Hill; 2001;p. 3935–3962
  2. Beckett D, Mathews BW. Escherichia coli repressor of biotin biosynthesis. Methods Enzymol. 1997;279:362–376
  3. Brown PH, Cronan JE, Grotli M, Beckett D. The biotin repressor: modulation of allostery by corepressor analogs. J Mol Biol. 2004;337:857–869
  4. Rodriguez-Melendez R, Cano S, Mendez ST, Velazquez A. Biotin regulates the genetic expression of holocarboxylase synthetase and mitochondrial carboxylases in rats. J Nutr. 2001;131:1909–1913
  5. Solorzano-Vargas RS, Pacheco-Alvarez D, Leon-Del-Rio A. Holocarboxylase synthetase is an obligate participant in biotin-mediated regulation of its own expression and of biotin-dependent carboxylases mRNA levels in human cells. Proc Natl Acad Sci U S A. 2002;99:5325–5330
  6. Dakshinamurti K. Vitamin receptors: vitamins as ligands in cell communication. Cambridge: Cambridge Univ Press; 1994;
  7. Rodriguez-Melendez R, Zempleni J. Regulation of gene expression by biotin. J Nutr Biochem. 2003;14:680–690
  8. Dakshinamurti K, Cheah-Tan C. Biotin-mediated synthesis of hepatic glucokinase in the rat. Arch Biochem Biophys. 1968;127:17–21
  9. Chauhan J, Dakshinamurti K. Transcriptional regulation of the glucokinase gene by biotin in starved rats. J Biol Chem. 1991;266:10035–10038
  10. Romero-Navarro G, Cabrera-Valladares G, German MS, Matschinsky FM, Velazquez A, Wang J, et al. Biotin regulation of pancreatic glucokinase and insulin in primary cultured rat islets and in biotin-deficient rats. Endocrinology. 1999;140:4595–4600
  11. Fernandez-Mejia C. Regulation of glucokinase by vitamins and hormones. In:  Matschinsky FM,  Magnuson MA editor. Glucokinase and glycemic disease: from basics to novel therapeutics. Front diabetes. Basel: Karger; 2004;p. 240–248
  12. Dakshinamurti K, Li W. Transcriptional regulation of liver phosphoenolpyruvate carboxykinase by biotin in diabetic rats. Mol Cell Biochem. 1994;132:127–132
  13. Spence JT, Koudelka AP. Effects of biotin upon the intracellular level of cGMP and the activity of glucokinase in cultured rat hepatocytes. J Biol Chem. 1984;259:6393–6396
  14. Hymes J, Fleischhauer K, Wolf B. Biotinylation of histones by human serum biotinidase: assessment of biotinyl-transferase activity in sera from normal individuals and children with biotinidase deficiency. Biochem Mol Med. 1995;56:76–83
  15. Zempleni J, Mock DM. Chemical synthesis of biotinylated histones and analysis by sodium dodecyl sulfate–polyacrylamide gel electrophoresis/streptavidin-peroxidase. Arch Biochem Biophys. 1999;371:83–88
  16. Stanley JS, Griffin JB, Zempleni J. Biotinylation of histones in human cells. Effects of cell proliferation. Eur J Biochem. 2001;268:5424–5429
  17. Narang MA, Dumas R, Ayer LM, Gravel RA. Reduced histone biotinylation in multiple carboxylase deficiency patients: a nuclear role for holocarboxylase synthetase. Hum Mol Genet. 2004;13:15–23
  18. Kothapalli N, Camporeale G, Kueh A, Chew YC, Oommen AM, Griffin JB, et al. Biological functions of biotinylated histones. J Nutr Biochem. 2005;[in press]
  19. Sherman F. Getting started with yeast. In:  Guthrie C,  Fink GR editor. Guide to yeast genetics and molecular and cell biology, part A. Amsterdam: Elsevier; 2004;p. 3–21
  20. Pérez-Vázquez V, Saavedra-Molina A, Uribe S. In Saccharomyces cerevisiae, cations control the fate of the energy derived from oxidative metabolism through the opening and closing of the yeast mitochondrial unselective channel. J Bioenerg Biomembr. 2003;35:231–241
  21. Brewster NK, Val DL, Walker ME, Wallace JC. Regulation of pyruvate carboxylase isozyme (PYC1, PYC2) gene expression in Saccharomyces cerevisiae during fermentative and nonfermentative growth. Arch Biochem Biophys. 1994;311:62–71
  22. Rodriguez-Melendez R, Perez-Andrade ME, Diaz A, Deolarte A, Camacho-Arroyo I, Ciceron I, et al. Differential effects of biotin deficiency and replenishment on rat liver pyruvate and propionyl-CoA carboxylases and on their mRNAs. Mol Genet Metab. 1999;66:16–23
  23. Kim HS, Hoja U, Stolz J, Sauer G, Schweizer E. Identification of the tRNA-binding protein Arc1p as a novel target of in vivo biotinylation in Saccharomyces cerevisiae. J Biol Chem. 2004;279:42445–42452

 This paper was presented at the “International Symposium: Vitamins as Regulators of Genetic Expression: Biotin as a Model” NAFTA Satellite Meeting to the XXV National Congress of Biochemistry held December 3–4, 2004, in Ixtapa, Zihuatanejo, Mexico. This meeting was sponsored by Sociedad Mexicana de Bioquimica A.C.; Programa de Doctorado en Ciencias Biomedicas, Universidad Nacional Autonoma de Mexico; Laboratorios Roche-Syntex, Mexico; and Instituto de Investigaciones Biomedicas, Universidad Nacional Autonoma de Mexico.

PII: S0955-2863(05)00096-3

doi: 10.1016/j.jnutbio.2005.03.023

The Journal of Nutritional Biochemistry
Volume 16, Issue 7 , Pages 438-440 , July 2005