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Published on August 4, 2006; 10.1104/pp.106.084004

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Received May 23, 2006
Accepted July 21, 2006

Chimeric Proteins Suggest that the Catalytic and/or C-terminal Domains Give CesA1 and CesA3 Access to their Specific Sites in the Cellulose Synthase of Primary Walls

Jian Wang , Paul A. Howles , Ann H. Cork , Rosemary J. Birch , and Richard E. Williamson *

Plant Cell Biology Group, Research School of Biological Sciences, Australian National University, Canberra, ACT 2601, Australia

* Corresponding author; email: richard.williamson{at}anu.edu.au.

CesA1 and CesA3 are thought to occupy non-interchangeable sites in the cellulose synthase making primary wall cellulose in Arabidopsis thaliana L. Heyn. With domain swaps and deletions we show that sites C-terminal to transmembrane domain 2 give CesAs access to their individual sites and, from dominance and recessive behaviour, deduce that certain CesA alleles exclude others from accessing each site. Constructs that swapped or deleted N-terminal domains were stably transformed into wild type and into the temperature-sensitive mutants rsw1 (Ala549Val in CesA1) and rsw5 (Pro1056Ser in CesA3). Dominant positive behaviour was assayed as root elongation at the restrictive temperature and dominant negative effects observed at the permissive temperature. A protein with the catalytic and C-terminal domains of CesA1 and the N-terminal domain of CesA3 promoted growth only in rsw1 consistent with it accessing the CesA1 site even though it contained the CesA3 N-terminal domain. A protein having the CesA3 catalytic and C-terminal domains linked to the CesA1 N-terminal domain dramatically affected growth but only in the CesA3 mutant. This is consistent with operation of the same access rule taking this chimeric protein to the CesA3 site. In this case, however, the transgene behaved as a genotype-specific, dominant negative, causing a 60% death rate in rsw5 but giving no visible phenotype in wild type or rsw1. We therefore hypothesise that their possession of CesA3WT protects Columbia and rsw1 from the lethal effects of this chimeric protein whereas the mutant protein (CesA3rsw5) does not.




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J. Wang, J. E. Elliott, and R. E. Williamson
Features of the primary wall CESA complex in wild type and cellulose-deficient mutants of Arabidopsis thaliana
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