Previous Article | Next Article 
Journal of Bacteriology, July 2006, p. 5266-5272, Vol. 188, No. 14
0021-9193/06/$08.00+0 doi:10.1128/JB.01566-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
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-Romero1*
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.
* Corresponding author. Mailing address for Javier Pozueta-Romero: Agrobioteknologiako Instituta, Nafarroako Unibertsitate Publikoa and Consejo Superior de Investigaciones Científicas, Mutiloako etorbidea zenbaki gabe, 31192 Mutiloabeti, Nafarroa, Spain. Phone: (34) 948168009. Fax: (34) 948232191. E-mail:
javier.pozueta{at}unavarra.es. Mailing address for Steven Ball: UMR8576 CNRS, Unversité de Lille, Villeneuve dAscq, France. E-mail: steven.ball@univ-lille1.fr.
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.
Journal of Bacteriology, July 2006, p. 5266-5272, Vol. 188, No. 14
0021-9193/06/$08.00+0 doi:10.1128/JB.01566-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
This article has been cited by other articles:
-
Matic, J. N., Terry, T. D., Van Bockel, D., Maddocks, T., Tinworth, D., Jennings, M. P., Djordjevic, S. P., Walker, M. J.
(2009). Development of Non-Antibiotic-Resistant, Chromosomally Based, Constitutive and Inducible Expression Systems for aroA-Attenuated Salmonella enterica Serovar Typhimurium. Infect. Immun.
77: 1817-1826
[Abstract]
[Full Text]
-
Seibold, G. M., Wurst, M., Eikmanns, B. J.
(2009). Roles of maltodextrin and glycogen phosphorylases in maltose utilization and glycogen metabolism in Corynebacterium glutamicum. Microbiology
155: 347-358
[Abstract]
[Full Text]
-
Jones, S. A., Jorgensen, M., Chowdhury, F. Z., Rodgers, R., Hartline, J., Leatham, M. P., Struve, C., Krogfelt, K. A., Cohen, P. S., Conway, T.
(2008). Glycogen and Maltose Utilization by Escherichia coli O157:H7 in the Mouse Intestine. Infect. Immun.
76: 2531-2540
[Abstract]
[Full Text]
-
Deschamps, P., Moreau, H., Worden, A. Z., Dauvillee, D., Ball, S. G.
(2008). Early Gene Duplication Within Chloroplastida and Its Correspondence With Relocation of Starch Metabolism to Chloroplasts. Genetics
178: 2373-2387
[Abstract]
[Full Text]
-
Lemonnier, M., Levin, B. R, Romeo, T., Garner, K., Baquero, M.-R., Mercante, J., Lemichez, E., Baquero, F., Blazquez, J.
(2008). The evolution of contact-dependent inhibition in non-growing populations of Escherichia coli. Proc R Soc B
275: 3-10
[Abstract]
[Full Text]
-
Patrauchan, M. A., Sarkisova, S. A., Franklin, M. J.
(2007). Strain-specific proteome responses of Pseudomonas aeruginosa to biofilm-associated growth and to calcium. Microbiology
153: 3838-3851
[Abstract]
[Full Text]
-
Edner, C., Li, J., Albrecht, T., Mahlow, S., Hejazi, M., Hussain, H., Kaplan, F., Guy, C., Smith, S. M., Steup, M., Ritte, G.
(2007). Glucan, Water Dikinase Activity Stimulates Breakdown of Starch Granules by Plastidial beta-Amylases. Plant Physiol.
145: 17-28
[Abstract]
[Full Text]
-
Seibold, G. M., Eikmanns, B. J.
(2007). The glgX gene product of Corynebacterium glutamicum is required for glycogen degradation and for fast adaptation to hyperosmotic stress. Microbiology
153: 2212-2220
[Abstract]
[Full Text]
-
Seibold, G., Dempf, S., Schreiner, J., Eikmanns, B. J.
(2007). Glycogen formation in Corynebacterium glutamicum and role of ADP-glucose pyrophosphorylase. Microbiology
153: 1275-1285
[Abstract]
[Full Text]