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J. Biol. Chem., Vol. 276, Issue 14, 11272-11278, April 6, 2001
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From the Hydroxyproline (Hyp) O-glycosylation
characterizes the hydroxyproline-rich glycoprotein (HRGP) superfamily
of the plant extracellular matrix. Hyp glycosylation occurs in two
modes: Arabinosylation adds short oligoarabinosides (Hyp-arabinosides)
while galactosylation leads to the addition of larger arabinogalactan
polysaccharides (Hyp-polysaccharides). We hypothesize that
sequence-dependent glycosylation of small peptide motifs
results in glycomodules. These small functional units in combination
with other repetitive peptide modules define the properties of HRGPs.
The Hyp contiguity hypothesis predicts arabinosylation of contiguous
Hyp residues and galactosylation of clustered noncontiguous Hyp
residues. To determine the minimum level of Hyp contiguity that directs
arabinosylation, we designed a series of synthetic genes encoding
repetitive (Ser-Pro2)n, (Ser-Pro3)n, and
(Ser-Pro4)n. A signal sequence targeted
these endogenous substrates to the endoplasmic reticulum/Golgi for
post-translational proline hydroxylation and glycosylation in
transformed Nicotiana tabacum cells. The fusion
glycoproteins also contained green fluorescence protein, facilitating
their detection and isolation. The (Ser-Pro2)n and
(Ser-Hyp4)n fusion glycoproteins yielded
Hyp-arabinosides but no Hyp-polysaccharide. The motif
(Ser-Pro3)n was incompletely hydroxylated, yielding
mixed contiguous/noncontiguous Hyp and a corresponding mixture of
Hyp-arabinosides and Hyp-polysaccharides. These results plus
circular dichroic spectra of the glycosylated and deglycosylated (Ser-Pro2)n, (Ser-Pro3)n, and
(Ser-Pro4)n modules corroborate the Hyp contiguity
hypothesis and indicate that Hyp O-glycosylation is indeed
sequence-driven.
Contiguous Hydroxyproline Residues Direct
Hydroxyproline Arabinosylation in Nicotiana tabacum*
,,¶
Department of Chemistry and Biochemistry,
Ohio University, Athens, Ohio 45701 and the § Department of
Biochemistry, Michigan State University, East Lansing, Michigan
48824
*
This work was supported by Grant MCB-9874744 from the
National Science Foundation and by grants from The Ohio Plant
Biotechnology Consortium and The Ohio University Early Stage
Development Fund.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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