NAD+-dependent post-translational modification of Escherichia coli glyceraldehyde-3-phosphate dehydrogenase.
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a multifunctional housekeeping protein reported to be a target of several covalent modifications in many organisms. In a previous study, enterohemorrhagic (EHEC) and enteropathogenic (EPEC) Escherichia coli strains were shown to secrete GAPDH and the protein to bind human plasminogen and fibrinogen. Here we report that GAPDH of these pathogens is ADP-ribosylated either in the cytoplasm or in the extracellular medium. GAPDH catalyzes its own modification, which involves Cys-149 at the active site. ADP-ribosylation of extracellular GAPDH may play an important role in the host-pathogen interaction, as also proposed in other pathogens.
Department of Biochemistry and Molecular Biology, Institute of Biomedicine of the University of Barcelona (IBUB), Faculty of Pharmacy, University of Barcelona, Barcelona, Spain.
Laura
L
Aguilera
Rosa
R
Giménez
Josefa
J
Badia
Juan
J
Aguilar
Laura
L
Baldoma
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism; D000595:Amino Acid Sequence; D054324:Enterohemorrhagic Escherichia coli / Q000201:enzymology* / Q000378:metabolism*; D054308:Enteropathogenic Escherichia coli / Q000201:enzymology* / Q000378:metabolism*; D024581:Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational
D000246:Adenosine Diphosphate Ribose; D024581:Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)