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Mapping of two O ‐GlcNAc modification sites in the capsid protein of the potyvirus Plum pox virus
Author(s) -
de Jesús Pérez José,
Juárez Silvia,
Chen Dinghu,
Scott Cheryl L.,
Hartweck Lynn M.,
Olszewski Neil E.,
García Juan Antonio
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.09.041
Subject(s) - capsid , pox virus , potyvirus , biology , virology , virus , glycoprotein , chemistry , biochemistry , plant 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 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.