title: Molecular characterisation of a cDNA sequence encoding the backbone of a style-specific 120 kDa glycoprotein which has features of both extensins and arabinogalactan proteins.
abstract: Nicotiana alata has a style-specific hydroxyproline-rich glycoprotein (the 120 kDa glycoprotein) which has properties of both extensins and AGPs [19, 20]. The 120 kDa glycoprotein is a soluble component in the extracellular matrix of the transmitting tract of styles where it accounts for ca. 9% of the total buffer-soluble protein. Here we describe the molecular cloning of a cDNA representing the gene NaPRP5 which encodes the backbone of the 120 kDa glycoprotein. Expression of mRNA is restricted to styles, consistent with observations on the distribution of the 120 kDa glycoprotein. Levels of accumulation of the transcript encoding the 120 kDa protein backbone are not altered significantly by pollination with either compatible or incompatible pollen. The protein backbone of the 120 kDa glycoprotein, as predicted by the cDNA sequence, is composed of three distinct domains. The sequence of these domains, together with linkage analysis of the carbohydrate component of the 120 kDa glycoprotein, allows predictions of the likely distribution of substituent glycosyl chains along the protein backbone. The similarity of the C-terminal domains of the 120 kDa glycoprotein and GaRSGP, the galactose-rich style glycoprotein of N. alata, is consistent with the two molecules sharing a common antigenic domain in their backbones [31]. The sharing of domains between distinct hydroxyproline-rich glycoproteins suggests that identification of a glycoprotein of this class solely by its protein or carbohydrate epitope is not valid.
authors.affiliation: CRC for Industrial Plant Biopolymers, School of Botany, University of Melbourne, Parkville, Vic., Australia.
authors.forename: C J
authors.initials: CJ
authors.lastname: Schultz
authors.forename: K
authors.initials: K
authors.lastname: Hauser
authors.forename: J L
authors.initials: JL
authors.lastname: Lind
authors.forename: A H
authors.initials: AH
authors.lastname: Atkinson
authors.forename: Z Y
authors.initials: ZY
authors.lastname: Pu
authors.forename: M A
authors.initials: MA
authors.lastname: Anderson
authors.forename: A E
authors.initials: AE
authors.lastname: Clarke
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000737:chemistry*; D005306:Fertilization; D018507:Gene Expression Regulation, Developmental; D018506:Gene Expression Regulation, Plant; D006023:Glycoproteins / Q000737:chemistry* / Q000235:genetics* / Q000302:isolation & purification; D006909:Hydroxyproline / Q000737:chemistry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009088:Mucoproteins / Q000737:chemistry*; D009928:Organ Specificity / Q000235:genetics; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification; D010947:Plants, Toxic; D011058:Pollen / Q000502:physiology; D017386:Sequence Homology, Amino Acid; D014026:Nicotiana / Q000235:genetics / Q000502:physiology; D014158:Transcription, Genetic / Q000502:physiology
chemical_list: D018076:DNA, Complementary; D006023:Glycoproteins; D009088:Mucoproteins; C109817:NaPRP5 protein, Nicotiana alata; D010940:Plant Proteins; C006619:arabinogalactan proteins; C005488:extensin protein, plant; D006909:Hydroxyproline