scholarly journals Cellulose Microfibril Formation by Surface-Tethered Cellulose Synthase Enzymes

ACS Nano ◽  
2016 ◽  
Vol 10 (2) ◽  
pp. 1896-1907 ◽  
Author(s):  
Snehasish Basu ◽  
Okako Omadjela ◽  
David Gaddes ◽  
Srinivas Tadigadapa ◽  
Jochen Zimmer ◽  
...  
2018 ◽  
Vol 177 (1) ◽  
pp. 151-167 ◽  
Author(s):  
Manoj Kumar ◽  
Laxmi Mishra ◽  
Paul Carr ◽  
Michael Pilling ◽  
Peter Gardner ◽  
...  

Science ◽  
2020 ◽  
Vol 369 (6507) ◽  
pp. 1089-1094 ◽  
Author(s):  
Pallinti Purushotham ◽  
Ruoya Ho ◽  
Jochen Zimmer

Cellulose is an essential plant cell wall component and represents the most abundant biopolymer on Earth. Supramolecular plant cellulose synthase complexes organize multiple linear glucose polymers into microfibrils as load-bearing wall components. We determined the structure of a poplar cellulose synthase CesA homotrimer that suggests a molecular basis for cellulose microfibril formation. This complex, stabilized by cytosolic plant-conserved regions and helical exchange within the transmembrane segments, forms three channels occupied by nascent cellulose polymers. Secretion steers the polymers toward a common exit point, which could facilitate protofibril formation. CesA’s N-terminal domains assemble into a cytosolic stalk that interacts with a microtubule-tethering protein and may thus be involved in CesA localization. Our data suggest how cellulose synthase complexes assemble and provide the molecular basis for plant cell wall engineering.


2010 ◽  
Vol 38 (3) ◽  
pp. 755-760 ◽  
Author(s):  
Raymond Wightman ◽  
Simon Turner

The potential for using cellulosic biomass as a source of fuel has renewed interest into how the large cellulose synthase complex deposits cellulose within the woody secondary walls of plants. This complex sits within the plasma membrane where it synthesizes numerous glucan chains which bond together to form the strong cellulose microfibril. The maintenance and guidance of the complex at the plasma membrane and its delivery to sites of secondary wall formation require the involvement of the cytoskeleton. In the present paper, we discuss the dynamics of the complex at the cell cortex and what is known about its assembly and trafficking.


Author(s):  
Simon Turner ◽  
Manoj Kumar

Cellulose consists of linear chains of β-1,4-linked glucose units, which are synthesized by the cellulose synthase complex (CSC). In plants, these chains associate in an ordered manner to form the cellulose microfibrils. Both the CSC and the local environment in which the individual chains coalesce to form the cellulose microfibril determine the structure and the unique physical properties of the microfibril. There are several recent reviews that cover many aspects of cellulose biosynthesis, which include trafficking of the complex to the plasma membrane and the relationship between the movement of the CSC and the underlying cortical microtubules (Bringmann et al. 2012 Trends Plant Sci. 17 , 666–674 ( doi:10.1016/j.tplants.2012.06.003 ); Kumar & Turner 2015 Phytochemistry 112 , 91–99 ( doi:10.1016/j.phytochem.2014.07.009 ); Schneider et al. 2016 Curr. Opin. Plant Biol. 34 , 9–16 ( doi:10.1016/j.pbi.2016.07.007 )). In this review, we will focus on recent advances in cellulose biosynthesis in plants, with an emphasis on our current understanding of the structure of individual catalytic subunits together with the local membrane environment where cellulose synthesis occurs. We will attempt to relate this information to our current knowledge of the structure of the cellulose microfibril and propose a model in which variations in the structure of the CSC have important implications for the structure of the cellulose microfibril produced. This article is part of a discussion meeting issue ‘New horizons for cellulose nanotechnology’.


2012 ◽  
Vol 109 (11) ◽  
pp. 4098-4103 ◽  
Author(s):  
D. M. Harris ◽  
K. Corbin ◽  
T. Wang ◽  
R. Gutierrez ◽  
A. L. Bertolo ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document