Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/117126
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Type: Journal article
Title: Cellulose microfibril crystallinity is reduced by mutating C-terminal transmembrane region residues CESA1A903V and CESA3T942I of cellulose synthase
Author: Harris, D.
Corbin, K.
Wang, T.
Gutierrez, R.
Bertolo, A.
Petti, C.
Smilgies, D.-M.
Estevez, J.
Bonetta, D.
Urbanowicz, B.
Ehrhardt, D.
Somerville, C.
Rose, J.
Hong, M.
DeBolt, S.
Citation: Proceedings of the National Academy of Sciences of USA, 2012; 109(11):4098-4103
Publisher: National Academy of Sciences of the United States of America
Issue Date: 2012
ISSN: 0027-8424
1091-6490
Statement of
Responsibility: 
Darby M. Harris, Kendall Corbin, Tuo Wang, Ryan Gutierrez, Ana L. Bertolo, Carloalberto Petti ... et al.
Abstract: The mechanisms underlying the biosynthesis of cellulose in plants are complex and still poorly understood. A central question concerns the mechanism of microfibril structure and how this is linked to the catalytic polymerization action of cellulose synthase (CESA). Furthermore, it remains unclear whether modification of cellulose microfibril structure can be achieved genetically, which could be transformative in a bio-based economy. To explore these processes in planta, we developed a chemical genetic toolbox of pharmacological inhibitors and corresponding resistance-conferring point mutations in the C-terminal transmembrane domain region of CESA1A903V and CESA3T942I in Arabidopsis thaliana. Using 13C solid-state nuclear magnetic resonance spectroscopy and X-ray diffraction, we show that the cellulose microfibrils displayed reduced width and an additional cellulose C4 peak indicative of a degree of crystallinity that is intermediate between the surface and interior glucans of wild type, suggesting a difference in glucan chain association during microfibril formation. Consistent with measurements of lower microfibril crystallinity, cellulose extracts from mutated CESA1A903V and CESA3T942I displayed greater saccharification efficiency than wild type. Using live-cell imaging to track fluorescently labeled CESA, we found that these mutants show increased CESA velocities in the plasma membrane, an indication of increased polymerization rate. Collectively, these data suggest that CESA1A903V and CESA3T942I have modified microfibril structure in terms of crystallinity and suggest that in plants, as in bacteria, crystallization biophysically limits polymerization.
Keywords: cell wall; polysaccharide; quinoxyphen
Rights: The author(s) retains copyright to individual PNAS articles, and the National Academy of Sciences of the United States of America (NAS) holds copyright to the collective work and retains an exclusive License to Publish these articles, except for open access articles submitted beginning September 2017. For such open access articles, NAS retains a nonexclusive License to Publish, and these articles are distributed under either a CC BY-NC-ND or CC BY license.
DOI: 10.1073/pnas.1200352109
Appears in Collections:Agriculture, Food and Wine publications
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