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Mapping of two O-GlcNAc modification sites in the capsid protein of the potyvirus Plum pox virus

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 th...

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Published in:FEBS letters 2006-10, Vol.580 (25), p.5822-5828
Main Authors: Pérez, José de Jesús, Juárez, Silvia, Chen, Dinghu, Scott, Cheryl L., Hartweck, Lynn M., Olszewski, Neil E., García, Juan Antonio
Format: Article
Language:English
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2006.09.041