Artículo

Abstract:

Potato (Solanum tuberosum L.) tuber UDP-glucose:protein transglucosylase (UPTG) (EC 2.4.1.112) is involved in the first of a two-step mechanism proposed for protein-bound α-glucan synthesis by catalyzing the covalent attachment of a single glucose residue to an acceptor protein. The resulting glucosylated 38-kilodalton polypeptide would then serve as a primer for enzymic glucan chain elongation during the second step. In the present report, we describe the fast protein liquid chromatography purification of UPTG from a membrane pellet of potato tuber. An apparently close association of UPTG, phosphorylase, and starch synthase was observed under native conditions during different purification steps. Enrichment of a 38-kilodalton polypeptide was found throughout enzyme purification. It is now shown that the purified UPTG, with an apparent molecular mass of 38 kilodaltons, undergoes self-glucosylation in a UDP-glucose- and Mn2+-dependent reaction. Therefore, it is concluded that UPTG is the enzyme and at the same time the priming protein required for the biogenesis of protein-bound α-glucan in potato tuber.

Registro:

Documento: Artículo
Título:Potato tuber UDP-Glucose: Protein transglucosylase catalyzes its own glucosylation
Autor:Ardila, F.J.; Tandecarz, J.S.
Filiación:Inst. Invest. Bioquim. Fund. C., Fac. de Ciencias Exactas y Naturales, Consejo Nac. Invest. Cientfic./T., Patricias Argentinas 435, 1405 Buenos Aires, Argentina
Palabras clave:Solanum tuberosum; Tuberosum
Año:1992
Volumen:99
Número:4
Página de inicio:1342
Página de fin:1347
DOI: http://dx.doi.org/10.1104/pp.99.4.1342
Título revista:Plant Physiology
Título revista abreviado:Plant Physiol.
ISSN:00320889
CODEN:PLPHA
PDF:https://bibliotecadigital.exactas.uba.ar/download/paper/paper_00320889_v99_n4_p1342_Ardila.pdf
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00320889_v99_n4_p1342_Ardila

Referencias:

  • Chamberlain, J.P., Fluorographic detection of radioactivity in polyacrylamide gels with water soluble fluor, sodium salicilate (1970) Anal Biochem, 98, pp. 132-135
  • Kennedy, L.D., Kirkman, B.R., Lomako, J., Rodriguez, I.R., Whelan, W.J., The biogenesis of rabbit-muscle glycogen (1985) Membranes and Muscle, pp. 65-84. , MC Berman, W Gevers, LH Opie, eds, ICSU/IRL Press, Oxford
  • Kirschner, B., Hahn, H., Patatin, a major soluble protein of the potato (Solanum tuberosum L.) tuber is synthesized as a larger precursor (1986) Planta, 168, pp. 386-389
  • Laemmli, J.K., Cleavage of structural proteins during assembly of head bacteriophage T4 (1970) Nature, 227, pp. 680-685
  • Lavintman, N., Cardini, C.E., Effect of cetyltrimethylammonium bromide on the activity of particulate starch synthase from potato tuber (1972) Plant Physiol, 50, pp. 205-207
  • Lavintman, N., Cardini, C.E., Particulate UDP-Glucose: Protein transglucosylase from potato tuber (1973) FEBS Lett, 29, pp. 43-46
  • Lavintman, N., Tandecarz, J.S., Carceller, M., Mendiara, S., Cardini, C.E., Role of uridine diphosphate glucose in the biosynthesis of starch. Mechanism of formation and enlargement of a glucoproteic acceptor (1974) Eur J Biochem, 50, pp. 145-155
  • Lomako, J., Lomako, W.M., Whelan, W.J., A self glucosylating protein is the primer for rabbit muscle glycogen biosynthesis (1988) FASEB J, 2, pp. 3097-3103
  • Lowry, O.H., Rosebrough, J.J., Farr, A.L., Randall, R.J., Protein measurement with the Folin phenol reagent (1951) J Biol Chem, 193, pp. 265-271
  • Matern, H., Bolz, R., Matern, S., Isolation and characterization of UDP-glucose dolichyl-phosphate glucosyl transferase from human liver (1990) Eur J Biochem, 190, pp. 99-105
  • Moreno, S., Cardini, C.E., Tandecarz, J.S., α-Glucan synthesis on a protein primer, uridine diphosphoglucose:protein trans-glucosylase. I. Separation from starch synthase and phosphorylase and a study of its properties (1986) Eur J Biochem, 157, pp. 539-545
  • Moreno, S., Cardini, C.E., Tandecarz, J.S., α-Glucan synthesis on a protein primer. II. A reconstituted system for the formation of protein-bound α-glucan (1987) Eur J Biochem, 162, pp. 609-614
  • Moreno, S., Tandecarz, J.S., Potato tuber glucosyl transferases: Partial characterization of the solubilized enzymes (1982) FEBS Lett, 139, pp. 313-316
  • Oakley, B.R., Kirsch, D.R., Morris, N.R., A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels (1980) Anal Biochem, 105, pp. 361-363
  • Pitcher, J., Smythe, C., Campbell, D.G., Cohen, P., Identification of the 38 kDa subunit of rabbit skeletal muscle glycogen synthase as glycogenin (1987) Eur J Biochem, 169, pp. 497-502
  • Pitcher, J., Smythe, C., Cohen, P., Glycogenin is the priming glucosyltransferase required for the initiation of glycogen biosynthesis in rabbit skeletal muscle (1988) Eur J Biochem, 176, pp. 391-395
  • Preiss, J., Levi, C., Starch biosynthesis and degradation (1980) The Biochemistry of Plants, 3, pp. 371-423. , J Preiss, ed, Academic Press, Inc, New York
  • Quentmeier, H., Ingold, E., Seitz, H.U., Purification of an autocatalytic protein-glycosylating enzyme from cell suspensions of Daucus carota L (1987) Planta, 171, pp. 483-488
  • Rodriguez, I.R., Tandecarz, J.S., Kirkman, B.R., Whelan, W.J., Tyrosine glycosylation is involved in muscle glycogen synthesis (1986) ICSU Short Reports, 4, pp. 96-99
  • Rothschild, A., Tandecarz, J.S., Maize UDP-Glc: Protein transglucosylase catalyses its own glucosylation (1990) 26th National Meeting of the Argentine Society of Biochemical Research, , Mar del Plata, Argentina
  • Sivak, M.N., Tandecarz, J.S., Cardini, C.E., Studies on potato tuber phosphorylase-catalyzed reaction in the absence of an exogenous acceptor. I. Characterization and properties of the enzyme (1981) Arch Biochem Biophys, 212, pp. 525-536
  • Smythe, C., Villar-Palasi, C., Cohen, P., Structural and functional studies on rabbit liver glicogenin (1989) Eur J Biochem, 183, pp. 205-209
  • Soodsman, J.F., Nordlie, R.C., Effects of cetyltrimethylammonium bromide on catalytic properties of kidney microsomal glucose 6-phosphotransferase, inorganic pyrophosphate-glucose phosphotransferase and inorganic pyrophosphatase activities (1969) Biochem Biophys Acta, 191, pp. 636-643
  • Steup, M., Schachtele, C., Latzko, E., Purification of a non-chloroplastic α-glucan phosphorylase from spinach leaves (1980) Planta, 148, pp. 168-173
  • Tandecarz, J.S., Cardini, C.E., A two-step enzymatic formation of a glucoprotein in potato tuber (1978) Biochem Biophys Acta, 543, pp. 423-429
  • Tandecarz, J.S., Cardini, C.E., Effect of 1,5-gluconolactone on the formation of a glucoprotein in potato tuber (1979) Plant Sci Lett, 15, pp. 151-158
  • Thomas, J.A., Kaith, K., Schlender, K., Larner, J., A rapid filter paper assay for UDPglucose-glycogen glucosyltransferase, including an improved biosynthesis of UDP-14C-glucose (1968) Anal Biochem, 25, pp. 486-499

Citas:

---------- APA ----------
Ardila, F.J. & Tandecarz, J.S. (1992) . Potato tuber UDP-Glucose: Protein transglucosylase catalyzes its own glucosylation. Plant Physiology, 99(4), 1342-1347.
http://dx.doi.org/10.1104/pp.99.4.1342
---------- CHICAGO ----------
Ardila, F.J., Tandecarz, J.S. "Potato tuber UDP-Glucose: Protein transglucosylase catalyzes its own glucosylation" . Plant Physiology 99, no. 4 (1992) : 1342-1347.
http://dx.doi.org/10.1104/pp.99.4.1342
---------- MLA ----------
Ardila, F.J., Tandecarz, J.S. "Potato tuber UDP-Glucose: Protein transglucosylase catalyzes its own glucosylation" . Plant Physiology, vol. 99, no. 4, 1992, pp. 1342-1347.
http://dx.doi.org/10.1104/pp.99.4.1342
---------- VANCOUVER ----------
Ardila, F.J., Tandecarz, J.S. Potato tuber UDP-Glucose: Protein transglucosylase catalyzes its own glucosylation. Plant Physiol. 1992;99(4):1342-1347.
http://dx.doi.org/10.1104/pp.99.4.1342