By Eugene A. Nothnagel, Antony Bacic, A.E. Clarke

Arabinogalactan-proteins are allotted during the plant state and are found in leaves, stems, roots, floral elements, and seeds. on the subcellular point, AGPs are localized at the plasma membrane, within the mobilephone wall, in secretory and endocytotic pathway organelles, in stylar and root secretions and within the medium of cultured cells. The common distribution of AGPs shows that they practice very important capabilities. a selection of data concerning AGPs has been initiated and sustained via new experimental methods, together with the improvement of monoclonal antibody probes and cloning of cDNAs similar to middle polypeptides. Regulated expression and different facts issues to the involvement of AGPs in plant reproductive improvement, trend formation, and somatic embryogenesis, in addition to within the techniques of mobilephone department, mobilephone growth, and cellphone demise. AGPs even have an value to undefined. One instance is gum arabic, an exudate from Acacia senegal, a mix of AGPs and polysaccharides which has certain viscosity and emulsifying houses that experience resulted in many makes use of within the nutrients besides as different industries.

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Additional info for Cell and Developmental Biology of Arabinogalactan-Proteins

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Rapport, M. , 1962, The interaction ofglycosides and saccharide with antibody to the corresponding phenylazo glycosides, Biochem. J. 85: 383-388. , 1967, Precipitation of arabic acid and some seed polysaccharides by glycosyl-phenylazo dyes, Biochem. 1. 105: IC-2C. , 1998, Arabinogalactan-proteins from Nicotiana alata and Pyrus communis contain glycosylphosphatidylinositol membrane anchors, Proc. Natl. Acad. Sci. USA 95: 7921-7926. , 1996, Complement activating galactan chains in a pectic arabinogalactan (AGlIb-1) from the roots of Angelica acutiloba Kitagawa, Carbohydr.

Each major group of sequences is defined by conserved and specific amino acid motifs. Some amino acid motifs are only found in AGPs, whereas others are also characteristic of other molecules such as insect fasciclins. By acknowledging these similarities it might be possible to discern AGP function in plant cell development. The presence of multi-domain proteins, such as group 1 AGPs, may reflect their complex evolution and indicate their multi-functional properties. The presence of different genes could explain the number of localizations and functions proposed for AGPs as well as their implication in different signaling pathways.

In addition the presence of an Asn-rich domain similar to the C-terminal of the group 2 AGPs from Pyrus and Nicotiana also occurs in a Plasmodium falciparum antigen (Wahlgren et al 1986) and in genes from Dictyostelium discoideum (Han and Firtel 1998) and Synechocystis sp. (Kaneko et al 1996) that encode, respectively, proteins related to transcription factors and a hypothetical AGP-like molecule. The sequences of group 3 are dissimilar but include many identified AGP sequences in addition to ESTs.

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