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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 |
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Main Authors: | , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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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. |
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ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/j.febslet.2006.09.041 |