A Structural Study of CESA1 Catalytic Domain of Arabidopsis Cellulose Synthesis Complex [electronic resource] : Evidence for CESA Trimers
- Washington, D.C. : United States. Dept. of Energy. Office of Science, 2015. and Oak Ridge, Tenn. : Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy
- Physical Description:
- pages 123-135 : digital, PDF file
- Additional Creators:
- Oak Ridge National Laboratory, United States. Department of Energy. Office of Science, United States. Department of Energy. Office of Basic Energy Sciences, and United States. Department of Energy. Office of Scientific and Technical Information
- Restrictions on Access:
- Free-to-read Unrestricted online access
- In a cellulose synthesis complex a "rosette" shape is responsible for the synthesis of cellulose chains and their assembly into microfibrils within the cell walls of land plants and their charophyte algal progenitors. The number of cellulose synthase proteins in this large multisubunit transmembrane protein complex and the number of cellulose chains in a microfibril have been debated for many years. Our work reports a low resolution structure of the catalytic domain of CESA1 from Arabidopsis (Arabidopsis thaliana; AtCESA1CatD) determined by small-angle scattering techniques and provides the first experimental evidence for the self-assembly of CESA into a stable trimer in solution. The catalytic domain was overexpressed in Escherichia coli, and using a two-step procedure, it was possible to isolate monomeric and trimeric forms of AtCESA1CatD. Moreover, the conformation of monomeric and trimeric AtCESA1CatD proteins were studied using small-angle neutron scattering and small-angle x-ray scattering. A series of AtCESA1CatD trimer computational models were compared with the small-angle x-ray scattering trimer profile to explore the possible arrangement of the monomers in the trimers. Several candidate trimers were identified with monomers oriented such that the newly synthesized cellulose chains project toward the cell membrane. In these models, the class-specific region is found at the periphery of the complex, and the plant-conserved region forms the base of the trimer. Finally, this study strongly supports the "hexamer of trimers" model for the rosette cellulose synthesis complex that synthesizes an 18-chain cellulose microfibril as its fundamental product.
- Published through SciTech Connect., 11/10/2015., Plant Physiology (Bethesda) 170 1 ISSN 0032-0889 AM, and Venu Gopal Vandavasi; Daniel K. Putnam; Qiu Zhang; Loukas Petridis; William T. Heller; B. Tracy Nixon; Candace H. Haigler; Udaya Kalluri; Leighton Coates; Paul Langan; Jeremy C. Smith; Jens Meiler; Hugh O’Neill.
- Funding Information:
- AC05-00OR22725 and AC02-98CH10886
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