| Literature DB >> 23371948 |
Li Tan1, Stefan Eberhard, Sivakumar Pattathil, Clayton Warder, John Glushka, Chunhua Yuan, Zhangying Hao, Xiang Zhu, Utku Avci, Jeffrey S Miller, David Baldwin, Charles Pham, Ronald Orlando, Alan Darvill, Michael G Hahn, Marcia J Kieliszewski, Debra Mohnen.
Abstract
Plant cell walls are comprised largely of the polysaccharides cellulose, hemicellulose, and pectin, along with ∼10% protein and up to 40% lignin. These wall polymers interact covalently and noncovalently to form the functional cell wall. Characterized cross-links in the wall include covalent linkages between wall glycoprotein extensins between rhamnogalacturonan II monomer domains and between polysaccharides and lignin phenolic residues. Here, we show that two isoforms of a purified Arabidopsis thaliana arabinogalactan protein (AGP) encoded by hydroxyproline-rich glycoprotein family protein gene At3g45230 are covalently attached to wall matrix hemicellulosic and pectic polysaccharides, with rhamnogalacturonan I (RG I)/homogalacturonan linked to the rhamnosyl residue in the arabinogalactan (AG) of the AGP and with arabinoxylan attached to either a rhamnosyl residue in the RG I domain or directly to an arabinosyl residue in the AG glycan domain. The existence of this wall structure, named ARABINOXYLAN PECTIN ARABINOGALACTAN PROTEIN1 (APAP1), is contrary to prevailing cell wall models that depict separate protein, pectin, and hemicellulose polysaccharide networks. The modified sugar composition and increased extractability of pectin and xylan immunoreactive epitopes in apap1 mutant aerial biomass support a role for the APAP1 proteoglycan in plant wall architecture and function.Entities:
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Year: 2013 PMID: 23371948 PMCID: PMC3584541 DOI: 10.1105/tpc.112.107334
Source DB: PubMed Journal: Plant Cell ISSN: 1040-4651 Impact factor: 11.277