| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
|
|
|
|||||||
|
|||||||||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Papers In Press, published online ahead of print July 7, 2003
Molecular Biology, C.N.R.S. - University of Lyon, Lyon 69007
Corresponding Author: aj.cozzone{at}ibcp.fr
Autophosphorylation of protein-tyrosine kinases (PTKs) involved in exo- and capsular polysaccharide biosynthesis and transport has been observed in a number of Gram-negative and Gram-positive bacteria. However, besides their own phosphorylation, little is known about other substrates targeted by these protein-modifying enzymes. Here, we present evidence that the protein-tyrosine kinase Wzc of E. coli is able to phosphorylate an endogenous enzyme, UDP-glucose dehydrogenase (Ugd), which participates in the synthesis of the exopolysaccharide colanic acid. The process of phosphorylation of Ugd by Wzc was shown to be stimulated by previous autophosphorylation of Wzc on tyrosine 569. The phosphorylation of Ugd was demonstrated to actually occur on tyrosine and to result in a significant increase of its dehydrogenase activity. In addition, the phosphotyrosine-protein phosphatase Wzb, which is known to effectively dephosphorylate Wzc, exhibited only a low effect, if any, on the dephosphorylation of Ugd. These data were related to the recent observation that two other UDP-glucose dehydrogenases have been also shown to be phosphorylated by a PTK in the Gram-positive bacterium Bacillus subtilis. Comparative analysis of the activities of PTKs from Gram-negative and Gram-positive bacteria showed that they are regulated by different mechanisms which involve, respectively, either the autophosphorylation of kinases or their interaction with a membrane protein activator.
J. Biol. Chem, 10.1074/jbc.M305134200
Submitted on May 15, 2003
Revised on July 7, 2003
Accepted on July 7, 2003
Autophosphorylation of the Escherichia coli protein kinase Wzc regulates tyrosine phosphorylation of Ugd, a UDP-glucose dehydrogenase+
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  A. E. Smith, S.-H. Kim, F. Liu, W. Jia, E. Vinogradov, C. L. Gyles, and R. E. Bishop PagP Activation in the Outer Membrane Triggers R3 Core Oligosaccharide Truncation in the Cytoplasm of Escherichia coli O157:H7 J. Biol. Chem., February 15, 2008; 283(7): 4332 - 4343. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 E. Yavuz, S. Drouillard, E. Samain, I. Roberts, and B. Priem Glucuronylation in Escherichia coli for the bacterial synthesis of the carbohydrate moiety of nonsulfated HNK-1 Glycobiology, February 1, 2008; 18(2): 152 - 157. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Z. Minic, C. Marie, C. Delorme, J.-M. Faurie, G. Mercier, D. Ehrlich, and P. Renault Control of EpsE, the Phosphoglycosyltransferase Initiating Exopolysaccharide Synthesis in Streptococcus thermophilus, by EpsD Tyrosine Kinase J. Bacteriol., February 15, 2007; 189(4): 1351 - 1357. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
V. Molle, A. K. Brown, G. S. Besra, A. J. Cozzone, and L. Kremer The Condensing Activities of the Mycobacterium tuberculosis Type II Fatty Acid Synthase Are Differentially Regulated by Phosphorylation J. Biol. Chem., October 6, 2006; 281(40): 30094 - 30103. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
E. Lescop, Y. Hu, H. Xu, W. Hu, J. Chen, B. Xia, and C. Jin The Solution Structure of Escherichia coli Wzb Reveals a Novel Substrate Recognition Mechanism of Prokaryotic Low Molecular Weight Protein-tyrosine Phosphatases J. Biol. Chem., July 14, 2006; 281(28): 19570 - 19577. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D. Vigetti, M. Ori, M. Viola, A. Genasetti, E. Karousou, M. Rizzi, F. Pallotti, I. Nardi, V. C. Hascall, G. De Luca, et al. Molecular Cloning and Characterization of UDP-glucose Dehydrogenase from the Amphibian Xenopus laevis and Its Involvement in Hyaluronan Synthesis J. Biol. Chem., March 24, 2006; 281(12): 8254 - 8263. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 I. Mijakovic, D. Petranovic, B. Macek, T. Cepo, M. Mann, J. Davies, P. R. Jensen, and D. Vujaklija Bacterial single-stranded DNA-binding proteins are phosphorylated on tyrosine Nucleic Acids Res., March 20, 2006; 34(5): 1588 - 1596. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
H. Xu, B. Xia, and C. Jin Solution Structure of a Low-Molecular-Weight Protein Tyrosine Phosphatase from Bacillus subtilis J. Bacteriol., February 15, 2006; 188(4): 1509 - 1517. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Peleg, Y. Shifrin, O. Ilan, C. Nadler-Yona, S. Nov, S. Koby, K. Baruch, S. Altuvia, M. Elgrably-Weiss, C. M. Abe, et al. Identification of an Escherichia coli Operon Required for Formation of the O-Antigen Capsule J. Bacteriol., August 1, 2005; 187(15): 5259 - 5266. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
I. Mijakovic, L. Musumeci, L. Tautz, D. Petranovic, R. A. Edwards, P. R. Jensen, T. Mustelin, J. Deutscher, and N. Bottini In Vitro Characterization of the Bacillus subtilis Protein Tyrosine Phosphatase YwqE J. Bacteriol., May 15, 2005; 187(10): 3384 - 3390. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. Nesper, C. M. D. Hill, A. Paiment, G. Harauz, K. Beis, J. H. Naismith, and C. Whitfield Translocation of Group 1 Capsular Polysaccharide in Escherichia coli Serotype K30: STRUCTURAL AND FUNCTIONAL ANALYSIS OF THE OUTER MEMBRANE LIPOPROTEIN Wza J. Biol. Chem., December 12, 2003; 278(50): 49763 - 49772. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
