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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
Keywords: Escheríchia coli
Escherichia coli
Seqüència d'aminoàcids
Amino acid sequence
Issue Date: Sep-2009
Publisher: Spanish Society for Microbiology (SEM) and Viguera Editores SL
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.
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It is part of: International Microbiology, 2009, vol. 12, núm. 3, p. 187-192
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ISSN: 1139-6709
Appears in Collections:Articles publicats en revistes (Bioquímica i Biomedicina Molecular)

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