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PNAS 98 (10): 5916-5921

Copyright © 2001 by the National Academy of Sciences.


BRS1, a serine carboxypeptidase, regulates BRI1 signaling in Arabidopsis thaliana

Jia Li*, Kevin A. Lease*, Frans E. Tax{dagger}, and John C. Walker*,{ddagger}

*Division of Biological Sciences, University of Missouri, Columbia, MO 65211; and {dagger}Department of Molecular and Cellular Biology, University of Arizona, Tucson, AZ 85721

Received for publication February 8, 2001.

Abstract: Brassinosteroid-insensitive 1 (BRI1) of Arabidopsis thaliana encodes a cell surface receptor for brassinosteroids. Mutations in BRI1 severely affect plant growth and development. Activation tagging of a weak bri1 allele (bri1-5) resulted in the identification of a new locus, brs1-1D. BRS1 is predicted to encode a secreted carboxypeptidase. Whereas a brs1 loss-of-function allele has no obvious mutant phenotype, overexpression of BRS1 can suppress bri1 extracellular domain mutants. Genetic analyses showed that brassinosteroids and a functional BRI1 protein kinase domain are required for suppression. In addition, overexpressed BRS1 missense mutants, predicted to abolish BRS1 protease activity, failed to suppress bri1-5. Finally, the effects of BRS1 are selective: overexpression in either wild-type or two other receptor kinase mutants resulted in no phenotypic alterations. These results strongly suggest that BRS1 processes a protein involved in an early event in the BRI1 signaling.

{ddagger} To whom reprint requests should be addressed. E-mail: WalkerJ{at}

Edited by Clarence A. Ryan, Jr., Washington State University, Pullman, WA, and approved March 9, 2001

This paper was submitted directly (Track II) to the PNAS office.

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