RTM3, Which Controls Long-Distance Movement of Potyviruses, Is a Member of a New Plant Gene Family Encoding a Meprin and TRAF Homology Domain-Containing Protein

Author:

Cosson Patrick1,Sofer Luc1,Hien Le Quang1,Léger Valérie1,Schurdi-Levraud Valérie1,Whitham Steven A.1,Yamamoto Miki L.1,Gopalan Suresh1,Le Gall Olivier1,Candresse Thierry1,Carrington James C.1,Revers Frédéric1

Affiliation:

1. UMR Génomique, Diversité et Pouvoir Pathogène, INRA-Université Bordeaux 2, Institut de Biologie Végétale Moléculaire, 33883 Villenave d’Ornon, France (P.C., L.S., Q.H.L., V.S.-L., O.L.G., T.C., F.R.); UMR BIOGECO 1202, INRA, Equipe de Génétique, 33612 Cestas cedex, France (V.L.); and Center for Genome Research and Biocomputing, Oregon State University, Corvallis, Oregon 97331 (S.A.W., M.L.Y., S.G

Abstract

Abstract Restriction of long-distance movement of several potyviruses in Arabidopsis (Arabidopsis thaliana) is controlled by at least three dominant restricted TEV movement (RTM) genes, named RTM1, RTM2, and RTM3. RTM1 encodes a protein belonging to the jacalin family, and RTM2 encodes a protein that has similarities to small heat shock proteins. In this article, we describe the positional cloning of RTM3, which encodes a protein belonging to an undescribed protein family of 29 members that has a meprin and TRAF homology (MATH) domain in its amino-terminal region and a coiled-coil domain at its carboxy-terminal end. Involvement in the RTM resistance system is the first biological function experimentally identified for a member of this new gene family in plants. Our analyses showed that the coiled-coil domain is not only highly conserved between RTM3-homologous MATH-containing proteins but also in proteins lacking a MATH domain. The cluster organization of the RTM3 homologs in the Arabidopsis genome suggests the role of duplication events in shaping the evolutionary history of this gene family, including the possibility of deletion or duplication of one or the other domain. Protein-protein interaction experiments revealed RTM3 self-interaction as well as an RTM1-RTM3 interaction. However, no interaction has been detected involving RTM2 or the potyviral coat protein previously shown to be the determinant necessary to overcome the RTM resistance. Taken together, these observations strongly suggest the RTM proteins might form a multiprotein complex in the resistance mechanism to block the long-distance movement of potyviruses.

Publisher

Oxford University Press (OUP)

Subject

Plant Science,Genetics,Physiology

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