Back to the future with the AGP–Ca2+ flux capacitor
Author(s) -
Derek T. A. Lamport,
Péter Várnai,
Charlotte E. Seal
Publication year - 2014
Publication title -
annals of botany
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.567
H-Index - 176
eISSN - 1095-8290
pISSN - 0305-7364
DOI - 10.1093/aob/mcu161
Subject(s) - biology , biochemistry , cytosol , biophysics , arabinogalactan , periplasmic space , cell wall , microbiology and biotechnology , escherichia coli , gene , enzyme
Arabinogalactan proteins (AGPs) are ubiquitous in green plants. AGPs comprise a widely varied group of hydroxyproline (Hyp)-rich cell surface glycoproteins (HRGPs). However, the more narrowly defined classical AGPs massively predominate and cover the plasma membrane. Extensive glycosylation by pendant polysaccharides O-linked to numerous Hyp residues like beads of a necklace creates a unique ionic compartment essential to a wide range of physiological processes including germination, cell extension and fertilization. The vital clue to a precise molecular function remained elusive until the recent isolation of small Hyp-arabinogalactan polysaccharide subunits; their structural elucidation by nuclear magentic resonance imaging, molecular simulations and direct experiment identified a 15-residue consensus subunit as a β-1,3-linked galactose trisaccharide with two short branched sidechains each with a single glucuronic acid residue that binds Ca(2+) when paired with its adjacent sidechain.
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