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Glycogen Phosphorylase, the Product of the glgP Gene, Catalyzes Glycogen Breakdown by Removing Glucose Units from the Nonreducing Ends in Escherichia coli

Nora Alonso-Casajús,^1, David Dauvillée,^3, Alejandro Miguel Viale,² Francisco José Muñoz,¹ Edurne Baroja-Fernández,¹ María Teresa Morán-Zorzano,¹ Gustavo Eydallin,¹ Steven Ball,^3* and Javier Pozueta-Romero^1*

Agrobioteknologiako Instituta, Nafarroako Unibertsitate Publikoa and Consejo Superior de Investigaciones Científicas, Mutiloako etorbidea zenbaki gabe, 31192 Mutiloabeti, Nafarroa, Spain,¹ Instituto de Biología Molecular y Celular de Rosario, Dpto. de Microbiología, Fac. de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Suipacha 531, 2000 Rosario, Argentina,² UMR8576 CNRS, Université de Lille, 59655 Villeneuve d'Ascq, France³

Received 14 October 2005/ Accepted 7 May 2006

To understand the biological function of bacterial glycogen phosphorylase (GlgP), we have produced and characterized Escherichia coli cells with null or altered glgP expression. glgP deletion mutants (glgP) totally lacked glycogen phosphorylase activity, indicating that all the enzymatic activity is dependent upon the glgP product. Moderate increases of glycogen phosphorylase activity were accompanied by marked reductions of the intracellular glycogen levels in cells cultured in the presence of glucose. In turn, both glycogen content and rates of glycogen accumulation in glgP cells were severalfold higher than those of wild-type cells. These defects correlated with the presence of longer external chains in the polysaccharide accumulated by glgP cells. The overall results thus show that GlgP catalyzes glycogen breakdown and affects glycogen structure by removing glucose units from the polysaccharide outer chains in E. coli.

Supplemental material for this article may be found at http://jb.asm.org/.

N.A.-C. and D.D. have equally contributed to this work.

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