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oai:recercat.cat:2445/335502025-11-19T20:40:49Zcom_2072_1057col_2072_478781col_2072_478917

NAD+-dependent post-translational modification of Escherichia coli glyceraldehyde-3-phosphate dehydrogenase Aguilera Gil, Maria Laura Giménez Claudio, Rosa Badía Palacín, Josefa Aguilar Piera, Juan Baldomà Llavinés, Laura Escheríchia coli Enterobacteriàcies Proteïnes Escherichia coli Enterobacteriaceae Proteins Seqüència d'aminoàcids Amino acid sequence 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. 2013-01-25T16:50:14Z 2013-01-25T16:50:14Z 2009-09 2013-01-25T16:50:14Z info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Reproducció del document publicat a: http://dx.doi.org/10.2436/20.1501.01.97 International Microbiology, 2009, vol. 12, núm. 3, p. 187-192 http://dx.doi.org/10.2436/20.1501.01.97 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 info:eu-repo/semantics/openAccess Spanish Society for Microbiology (SEM) and Viguera Editores SL Articles publicats en revistes (Bioquímica i Biomedicina Molecular)