Identifying the ionically bound cell wall and intracellular glycoside hydrolases in late growth stage Arabidopsis stems: Implications for the genetic engineering of bioenergy crops
Abstract
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 CaCl2-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 has 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 thanmore »
- Authors:
-
- National Renewable Energy Lab. (NREL), Golden, CO (United States). Biosciences Center
- National Renewable Energy Lab. (NREL), Golden, CO (United States). Biosciences Center; Michigan State Univ., East Lansing, MI (United States). Dept. of Plant Biology
- National Renewable Energy Lab. (NREL), Golden, CO (United States). National Bioenergy Center
- Publication Date:
- Research Org.:
- National Renewable Energy Laboratory (NREL), Golden, CO (United States); Energy Frontier Research Centers (EFRC) (United States). Center for Direct Catalytic Conversion of Biomass to Biofuels (C3Bio)
- Sponsoring Org.:
- USDOE Office of Science (SC); USDOE Laboratory Directed Research and Development (LDRD) Program
- OSTI Identifier:
- 1220740
- Report Number(s):
- NREL/JA-2700-64209
Journal ID: ISSN 1664-462X
- Grant/Contract Number:
- SC0000997
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Frontiers in Plant Science
- Additional Journal Information:
- Journal Volume: 6; Journal ID: ISSN 1664-462X
- Publisher:
- Frontiers Research Foundation
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; 09 BIOMASS FUELS; cell wall proteins; glycoside hydrolase; xylan-modifying enzyme; pectin-modifying enzyme; plant late growth stage; plant senescence; biomass recalcitrance; feedstock engineering
Citation Formats
Wei, Hui, Brunecky, Roman, Donohoe, Bryon S., Ding, Shi -You, Ciesielski, Peter N., Yang, Shihui, Tucker, Melvin P., and Himmel, Michael E. Identifying the ionically bound cell wall and intracellular glycoside hydrolases in late growth stage Arabidopsis stems: Implications for the genetic engineering of bioenergy crops. United States: N. p., 2015.
Web. doi:10.3389/fpls.2015.00315.
Wei, Hui, Brunecky, Roman, Donohoe, Bryon S., Ding, Shi -You, Ciesielski, Peter N., Yang, Shihui, Tucker, Melvin P., & Himmel, Michael E. Identifying the ionically bound cell wall and intracellular glycoside hydrolases in late growth stage Arabidopsis stems: Implications for the genetic engineering of bioenergy crops. United States. https://doi.org/10.3389/fpls.2015.00315
Wei, Hui, Brunecky, Roman, Donohoe, Bryon S., Ding, Shi -You, Ciesielski, Peter N., Yang, Shihui, Tucker, Melvin P., and Himmel, Michael E. Wed .
"Identifying the ionically bound cell wall and intracellular glycoside hydrolases in late growth stage Arabidopsis stems: Implications for the genetic engineering of bioenergy crops". United States. https://doi.org/10.3389/fpls.2015.00315. https://www.osti.gov/servlets/purl/1220740.
@article{osti_1220740,
title = {Identifying the ionically bound cell wall and intracellular glycoside hydrolases in late growth stage Arabidopsis stems: Implications for the genetic engineering of bioenergy crops},
author = {Wei, Hui and Brunecky, Roman and Donohoe, Bryon S. and Ding, Shi -You and Ciesielski, Peter N. and Yang, Shihui and Tucker, Melvin P. and Himmel, Michael E.},
abstractNote = {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 CaCl2-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 has 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.},
doi = {10.3389/fpls.2015.00315},
journal = {Frontiers in Plant Science},
number = ,
volume = 6,
place = {United States},
year = {Wed May 13 00:00:00 EDT 2015},
month = {Wed May 13 00:00:00 EDT 2015}
}
Web of Science
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Combining various strategies to increase the coverage of the plant cell wall glycoproteome
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journal, November 2006
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Papaya β-galactosidase/galactanase isoforms in differential cell wall hydrolysis and fruit softening during ripening
journal, December 2004
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Heterologous expression of glycosyl hydrolases in planta: a new departure for biofuels
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