Characterization of hydroxyproline rich oligopeptides with AGP- and extensin-motifs expressed in Arabidospsis.

ESTEVEZ, J. M.; KIESLISZEWSKI M. J. & C. SOMERVILLE.

PLANT PHYSIOLOGY.

Año: 2006 vol. 142 p. 458 - 470

0032-0889

A series of gene constructs encoding synthetic glycomodule peptides with N-terminal signal sequences and C-terminal green fluorescent proteins were expressed in transgenic Arabidopsis under control of the 35S promoter. The synthetic glycomodule peptides were composed of repetitive proline-containing motifs that have been previously found to be substrates for prolyl hydroxylases and subsequent O-glycosylation of the hydroxyproline residues. All of the constructs were secreted in aerial tissues but not secreted in roots. The amount of hydroxylation and glycosylation of the various constructs varied depending on the tissue. Also, the accumulation of the proteins exhibited a high degree of cell-type specificity within various tissues due to post-transcriptional effects. The observations reveal a high level of complexity in the synthesis, secretion, and turnover of the glycoproteins. A series of gene constructs encoding synthetic glycomodule peptides with N-terminal signal sequences and C-terminal green fluorescent proteins were expressed in transgenic Arabidopsis under control of the 35S promoter. The synthetic glycomodule peptides were composed of repetitive proline-containing motifs that have been previously found to be substrates for prolyl hydroxylases and subsequent O-glycosylation of the hydroxyproline residues. All of the constructs were secreted in aerial tissues but not secreted in roots. The amount of hydroxylation and glycosylation of the various constructs varied depending on the tissue. Also, the accumulation of the proteins exhibited a high degree of cell-type specificity within various tissues due to post-transcriptional effects. The observations reveal a high level of complexity in the synthesis, secretion, and turnover of the glycoproteins. A series of gene constructs encoding synthetic glycomodule peptides with N-terminal signal sequences and C-terminal green fluorescent proteins were expressed in transgenic Arabidopsis under control of the 35S promoter. The synthetic glycomodule peptides were composed of repetitive proline-containing motifs that have been previously found to be substrates for prolyl hydroxylases and subsequent O-glycosylation of the hydroxyproline residues. All of the constructs were secreted in aerial tissues but not secreted in roots. The amount of hydroxylation and glycosylation of the various constructs varied depending on the tissue. Also, the accumulation of the proteins exhibited a high degree of cell-type specificity within various tissues due to post-transcriptional effects. The observations reveal a high level of complexity in the synthesis, secretion, and turnover of the glycoproteins.