NAD+ -dependent post-translational modification of Escherichia coli glyceraldehyde-3-phosphate dehydrogenase
Int. microbiol
; 12(3): 187-192, sept. 2009. ilus
Artigo
em Inglês
| IBECS
| ID: ibc-72379
Biblioteca responsável:
ES1.1
Localização: BNCS
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, 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 (AU)
RESUMEN
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Coleções:
Bases de dados nacionais
/
Espanha
Contexto em Saúde:
Doenças Negligenciadas
Problema de saúde:
Doenças Negligenciadas
/
Zoonoses
Base de dados:
IBECS
Assunto principal:
Gliceraldeído 3-Fosfato Desidrogenase (NADP/)
/
Escherichia coli
Idioma:
Inglês
Revista:
Int. microbiol
Ano de publicação:
2009
Tipo de documento:
Artigo
Instituição/País de afiliação:
University of Barcelona/Spain