Mapping of two O-GlcNAc modification sites in the capsid protein of the potyvirus Plum pox virus.
FEBS Lett
; 580(25): 5822-8, 2006 Oct 30.
Article
em En
| MEDLINE
| ID: mdl-17014851
ABSTRACT
A large number of O-linked N-acetylglucosamine (O-GlcNAc) residues have been mapped in vertebrate proteins, however targets of O-GlcNAcylation in plants still have not been characterized. We show here that O-GlcNAcylation of the N-terminal region of the capsid protein of Plum pox virus resembles that of animal proteins in introducing O-GlcNAc monomers. Thr-19 and Thr-24 were specifically O-GlcNAcylated. These residues are surrounded by amino acids typical of animal O-GlcNAc acceptor sites, suggesting that the specificity of O-GlcNAc transferases is conserved among plants and animals. In laboratory conditions, mutations preventing O-GlcNAcylation of Thr-19 and Thr-24 did not have noticeable effects on PPV competence to infect Prunus persicae or Nicotiana clevelandii. However, the fact that Thr-19 and Thr-24 are highly conserved among different PPV strains suggests that their O-GlcNAc modification could be relevant for efficient competitiveness in natural conditions.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Vírus Eruptivo da Ameixa
/
Proteínas do Capsídeo
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
2006
Tipo de documento:
Article
País de afiliação:
Espanha