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THE PLANT CELL, Vol 8, Issue 2 169-178, Copyright © 1996 by American Society of Plant Biologists
Identification of an Elicitor Active Site within the Three-Dimensional Structure of the Tobacco Mosaic Tobamovirus Coat Protein
Z. F. Taraporewala and J. N. Culver
Molecular and Cell Biology Program, University of Maryland, College Park, Maryland 20742
The coat protein (CP) of tobacco mosaic tobamovirus (TMV) elicits the
hypersensitive response (HR) conferred by the N[prime] gene from Nicotiana
sylvestris. This study presents evidence demonstrating a critical role for
a specific CP structural site in eliciting this HR. Based on the known
structure of the TMV CP, specific substitutions were created within the CP
of the elicitor strain P20L to identify structural areas essential for host
recognition. Of 32 substitutions made, 14 conferred either a
temperature-sensitive (loss of the HR at 29[deg]C) or a knockout (loss of
the HR at 25[deg]C) HR phenotype in N. sylvestris. These essential residues
were noncontiguous in position; however, within the three-dimensional CP
structure, all resided primarily along the right face of the molecule's
helical bundle. Substitutions that did not affect the HR phenotype either
were located outside of this area or were conservative in change. In
addition, placing two temperaturesensitive substitutions within the same CP
resulted in lowering temperature sensitivity from 29 to 27[deg]C. This
additive effect suggests that residues essential for HR elicitation
contribute independently to host recognition. This feature is
characteristic of recognition surfaces. The presence of a specific elicitor
active site within the three-dimensional structure of the TMV CP is
consistent with binding of a host-encoded receptor and demonstrates the
importance of CP structure in HR specificity.
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