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Title:	NAD+-dependent post-translational modification of Escherichia coli glyceraldehyde-3-phosphate dehydrogenase
Author:	Aguilera Gil, Maria Laura; Giménez Claudio, Rosa; Badía Palacín, Josefa; Aguilar Piera, Juan; Baldomà Llavinés, Laura
Other authors:	Universitat de Barcelona
Abstract:	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 we showed that enterohemorragic (EHEC) and enteropathogenic (EPEC) Escherichia coli strains secrete GAPDH and that this protein binds to 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 Cys149 at the active site. ADP-ribosylation of extracellular GAPDH may play important role in the interaction with the host as it has been proposed in other pathogens.
Subject(s):	-Escheríchia coli -Enterobacteriàcies -Proteïnes -Escherichia coli -Enterobacteriaceae -Proteins -Seqüència d'aminoàcids -Amino acid sequence
Rights:	cc-by-nc-sa (c) Spanish Society for Microbiology (SEM) and Viguera Editores SL, 2009 http://creativecommons.org/licenses/by-nc-sa/3.0/es
Document type:	Article Article - Published version
Published by:	Spanish Society for Microbiology (SEM) and Viguera Editores SL
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