2026-04-14T04:24:57Zhttps://recercat.cat/oai/request

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

00925njm 22002777a 4500 dc Aguilera Gil, Maria Laura author Giménez Claudio, Rosa author Badía Palacín, Josefa author Aguilar Piera, Juan author Baldomà Llavinés, Laura author 2013-01-25T16:50:14Z 2013-01-25T16:50:14Z 2009-09 2013-01-25T16:50:14Z 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. Escheríchia coli Enterobacteriàcies Proteïnes Escherichia coli Enterobacteriaceae Proteins Seqüència d'aminoàcids Amino acid sequence NAD+-dependent post-translational modification of Escherichia coli glyceraldehyde-3-phosphate dehydrogenase