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Plant Physiol, April 2001, Vol. 125, pp. 2180-2188
Class III Pistil-Specific Extensin-Like Proteins from Tobacco
Have Characteristics of Arabinogalactan Proteins
Maurice
Bosch,*
Jens Sommer
Knudsen,
Jan
Derksen, and
Celestina
Mariani
Graduate School of Experimental Plant Sciences, Department of
Experimental Botany, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands (M.B., J.D., C.M.); and Cooperative
Research Centre for Bioproducts, School of Botany, University of
Melbourne, Parkville 3052, Australia (J.S.K.)
Class III pistil-specific extensin-like proteins (PELPIII) are
specifically localized in the intercellular matrix of tobacco (Nicotiana tabacum) styles. After pollination the
majority of PELPIII are translocated into the callosic layer and the
callose plugs of the pollen tubes, which could suggest a function of
PELPIII in pollen tube growth. PELPIII may represent one of the
chemical and/or physical factors from the female sporophytic tissue
that contributes to the difference between in vivo and in vitro pollen tube growth. PELPIII glycoproteins were purified and biochemically characterized. Because of their high proline (Pro) and hydroxy-Pro (Hyp) content, PELPIII proteins belong to the class of Pro/Hyp-rich glycoproteins. The carbohydrate moiety of PELPIII is attached through
O-glycosidic linkages and comprises more than
one-half the total glycoprotein. Deglycosylation of PELPIII revealed
two backbones, both reacting with PELPIII-specific antibodies.
N-terminal amino acid sequencing of these backbones showed that PELPIII
is encoded by the MG14 and MG15 genes.
Two heterogeneous N-terminal sequences of MG14 and
MG15, both starting downstream of the predicted signal
peptide cleavage site, seem to be present, which indicates a novel
N-terminal processing. Monosaccharide analysis showed that the
carbohydrate moiety of PELPIII almost completely consists of arabinose
and galactose in an equal molar ratio. Carbohydrate linkage analysis
showed terminal and 2-linked arabinofuranosyl residues, as well as
terminal and 6-, 3-, and 3,6-linked galactopyranosyl residues to be
present, indicating the presence of both extensin-like and Type II
arabinogalactan oligosaccharide units. The ability of  -glucosyl
Yariv reagent to bind with PELPIII confirmed the arabinogalactan
protein-like characteristics of these proteins.
*
Corresponding author; e-mail mbosch{at}sci.kun.nl; fax
31-243652490.
© 2001 American Society of Plant Physiologists
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