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Title: Identifying Stable Fragments of Arabidopsis thaliana Cellulose Synthase Subunit 3 by Yeast Display

Abstract

Determining structures of large, complex proteins remains challenging, especially for transmembrane proteins, as the protein size increases. Additionally, Arabidopsis thaliana cellulose synthesis complex is a large, multimeric complex located in the plant cell membrane that synthesizes cellulose microfibrils in the plant cell wall. Despite the biological and economic importance of cellulose and therefore cellulose synthesis, many aspects of the cellulase synthase complex (CSC) structure and function are still unknown. Here, yeast surface display (YSD) is used to determine the full-length expression of A. thaliana cellulose synthase 3 (AtCesA3) fragments. The level of stably-folded AtCesA3 fragments displayed on the yeast surface are determined using flow cytometric analysis of differential surface expression of epitopes flanking the AtCesA3 fragment. This technique provides a fast and simple method for examining folding and expression of protein domains and fragments of complex proteins.

Authors:
 [1];  [1];  [1];  [1];  [2]; ORCiD logo [1]
+ Show Author Affiliations
  1. Univ. of Tennessee, Knoxville, TN (United States)
  2. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Center for Structural Molecular Biology (CSMB)
Publication Date:
Research Org.:
Energy Frontier Research Centers (EFRC) (United States). Center for Lignocellulose Structure and Formation (CLSF); Pennsylvania State Univ., University Park, PA (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES)
OSTI Identifier:
1767458
Alternate Identifier(s):
OSTI ID: 1473738
Grant/Contract Number:  
SC0001090; AC05-00OR22725; AC05‐00OR22725
Resource Type:
Accepted Manuscript
Journal Name:
Biotechnology Journal
Additional Journal Information:
Journal Volume: 14; Journal Issue: 4; Journal ID: ISSN 1860-6768
Publisher:
Wiley
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; biofuels (including algae and biomass); bio-inspired; membrane; carbon sequestration; materials and chemistry by design; synthesis (self-assembly); cellulose synthase; domain identification; library of random protein fragments; protein stability; yeast surface display

Citation Formats

Raeeszadeh‐Sarmazdeh, Maryam, Patel, Nikhil, Cruise, Sarah, Owen, Leila, O'Neill, Hugh, and Boder, Eric T. Identifying Stable Fragments of Arabidopsis thaliana Cellulose Synthase Subunit 3 by Yeast Display. United States: N. p., 2018. Web. doi:10.1002/biot.201800353.
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Raeeszadeh‐Sarmazdeh, Maryam, Patel, Nikhil, Cruise, Sarah, Owen, Leila, O'Neill, Hugh, & Boder, Eric T. Identifying Stable Fragments of Arabidopsis thaliana Cellulose Synthase Subunit 3 by Yeast Display. United States. https://doi.org/10.1002/biot.201800353
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Raeeszadeh‐Sarmazdeh, Maryam, Patel, Nikhil, Cruise, Sarah, Owen, Leila, O'Neill, Hugh, and Boder, Eric T. Sat . "Identifying Stable Fragments of Arabidopsis thaliana Cellulose Synthase Subunit 3 by Yeast Display". United States. https://doi.org/10.1002/biot.201800353. https://www.osti.gov/servlets/purl/1767458.
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@article{osti_1767458,
title = {Identifying Stable Fragments of Arabidopsis thaliana Cellulose Synthase Subunit 3 by Yeast Display},
author = {Raeeszadeh‐Sarmazdeh, Maryam and Patel, Nikhil and Cruise, Sarah and Owen, Leila and O'Neill, Hugh and Boder, Eric T.},
abstractNote = {Determining structures of large, complex proteins remains challenging, especially for transmembrane proteins, as the protein size increases. Additionally, Arabidopsis thaliana cellulose synthesis complex is a large, multimeric complex located in the plant cell membrane that synthesizes cellulose microfibrils in the plant cell wall. Despite the biological and economic importance of cellulose and therefore cellulose synthesis, many aspects of the cellulase synthase complex (CSC) structure and function are still unknown. Here, yeast surface display (YSD) is used to determine the full-length expression of A. thaliana cellulose synthase 3 (AtCesA3) fragments. The level of stably-folded AtCesA3 fragments displayed on the yeast surface are determined using flow cytometric analysis of differential surface expression of epitopes flanking the AtCesA3 fragment. This technique provides a fast and simple method for examining folding and expression of protein domains and fragments of complex proteins.},
doi = {10.1002/biot.201800353},
journal = {Biotechnology Journal},
number = 4,
volume = 14,
place = {United States},
year = {Sat Sep 01 00:00:00 EDT 2018},
month = {Sat Sep 01 00:00:00 EDT 2018}
}
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https://doi.org/10.1002/biot.201800353
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