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Title: Gradients in Wall Mechanics and Polysaccharides along Growing Inflorescence Stems

Authors:
; ; ; ORCiD logo; ; ORCiD logo; ORCiD logo
Publication Date:
Sponsoring Org.:
USDOE
OSTI Identifier:
1405564
Grant/Contract Number:
SC0001090
Resource Type:
Journal Article: Published Article
Journal Name:
Plant Physiology (Bethesda)
Additional Journal Information:
Journal Name: Plant Physiology (Bethesda); Journal Volume: 175; Journal Issue: 4; Related Information: CHORUS Timestamp: 2017-12-05 08:42:08; Journal ID: ISSN 0032-0889
Publisher:
American Society of Plant Biologists (ASPB)
Country of Publication:
United States
Language:
English

Citation Formats

Phyo, Pyae, Wang, Tuo, Kiemle, Sarah N., O’Neill, Hugh, Pingali, Sai Venkatesh, Hong, Mei, and Cosgrove, Daniel J. Gradients in Wall Mechanics and Polysaccharides along Growing Inflorescence Stems. United States: N. p., 2017. Web. doi:10.1104/pp.17.01270.
Phyo, Pyae, Wang, Tuo, Kiemle, Sarah N., O’Neill, Hugh, Pingali, Sai Venkatesh, Hong, Mei, & Cosgrove, Daniel J. Gradients in Wall Mechanics and Polysaccharides along Growing Inflorescence Stems. United States. doi:10.1104/pp.17.01270.
Phyo, Pyae, Wang, Tuo, Kiemle, Sarah N., O’Neill, Hugh, Pingali, Sai Venkatesh, Hong, Mei, and Cosgrove, Daniel J. 2017. "Gradients in Wall Mechanics and Polysaccharides along Growing Inflorescence Stems". United States. doi:10.1104/pp.17.01270.
@article{osti_1405564,
title = {Gradients in Wall Mechanics and Polysaccharides along Growing Inflorescence Stems},
author = {Phyo, Pyae and Wang, Tuo and Kiemle, Sarah N. and O’Neill, Hugh and Pingali, Sai Venkatesh and Hong, Mei and Cosgrove, Daniel J.},
abstractNote = {},
doi = {10.1104/pp.17.01270},
journal = {Plant Physiology (Bethesda)},
number = 4,
volume = 175,
place = {United States},
year = 2017,
month =
}

Journal Article:
Free Publicly Available Full Text
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  • Identifying the cell wall-ionically bound glycoside hydrolases (GHs) in Arabidopsis stems is important for understanding the regulation of cell wall integrity. For cell wall proteomics studies, the preparation of clean cell wall fractions is a challenge since cell walls constitute an open compartment, which is more likely to contain a mixture of intracellular and extracellular proteins due to cell leakage at the late growth stage. Here, for this study, we utilize a CaCl 2-extraction procedure to isolate non-structural proteins from Arabidopsis whole stems, followed by the in-solution and in-gel digestion methods coupled with Nano-LC-MS/MS, bioinformatics and literature analyses. This hasmore » led to the identification of 75 proteins identified using the in-solution method and 236 proteins identified by the in-gel method, among which about 10% of proteins predicted to be secreted. Together, eight cell wall proteins, namely AT1G75040, AT5G26000, AT3G57260, AT4G21650, AT3G52960, AT3G49120, AT5G49360, and AT3G14067, were identified by the in-solution method; among them, three were the GHs (AT5G26000, myrosinase 1, GH1; AT3G57260, β-1,3-glucanase 2, GH17; AT5G49360, bifunctional XYL 1/α-L-arabinofuranosidase, GH3). Moreover, four more GHs: AT4G30270 (xyloglucan endotransferase, GH16), AT1G68560 (bifunctional α-l-arabinofuranosidase/XYL, GH31), AT1G12240 (invertase, GH32) and AT2G28470 (β-galactosidase 8, GH35), were identified by the in-gel solution method only. Notably, more than half of above identified GHs are xylan- or hemicellulose-modifying enzymes, and will likely have an impact on cellulose accessibility, which is a critical factor for downstream enzymatic hydrolysis of plant tissues for biofuels production. Finally, the implications of these cell wall proteins identified at the late growth stage for the genetic engineering of bioenergy crops are discussed.« less
  • Monoclonal antibodies (McAbs) are useful tools to probe the structure of plant cell wall polysaccharides and to localize these polysaccharides in plant cells and tissues. Murine McAbs were generated against the pectic polysaccharide, rhamnogalacturonan I (RG-I), isolated from suspension-cultured sycamore cells. The McAbs that were obtained were grouped into three classes based upon their reactivities with a variety of plant polysaccharides and membrane glycoproteins. Eleven McAbs (Class I) recognize epitope(s) that appear to be immunodominant and are found in RG-I from sycamore and maize, citrus pectin, polygalacturonic acid, and membrane glycoproteins from suspension-cultured cells of sycamore, maize, tobacco, parsley, andmore » soybean. A second group of five McAbs (Class II) recognize epitope(s) present in sycamore RG-I, but do not bind to any of the other polysaccharides or glycoproteins recognized by Class I. Lastly, one McAb (Class III) reacts with sycamore RG-I, sycamore and tamarind xyloglucan, and sycamore and rice glucuronoarabinoxylan, but does not bind to maize RG-I, polygalacturonic acid or the plant membrane glycoproteins recognized by Class I. McAbs in Classes II and III are likely to be useful in studies of the structure, biosynthesis and localization of plant cell wall polysaccharides.« less