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PIRIN 2 stabilizes cysteine protease XCP 2 and increases susceptibility to the vascular pathogen Ralstonia solanacearum in Arabidopsis
Author(s) -
Zhang Bo,
Tremousaygue Dominique,
Denancé Nicolas,
Esse H. Peter,
Hörger Anja C.,
Dabos Patrick,
Goffner Deborah,
Thomma Bart P. H. J.,
Hoorn Renier A. L.,
Tuominen Hannele
Publication year - 2014
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/tpj.12602
Subject(s) - ralstonia solanacearum , arabidopsis , mutant , proteases , biology , cysteine protease , arabidopsis thaliana , cysteine , biochemistry , gene , pathogen , genetics , enzyme
Summary PIRIN ( PRN ) is a member of the functionally diverse cupin protein superfamily. There are four members of the Arabidopsis thaliana PRN family, but the roles of these proteins are largely unknown. Here we describe a function of the Arabidopsis PIRIN 2 ( PRN 2) that is related to susceptibility to the bacterial plant pathogen Ralstonia solanacearum . Two prn2 mutant alleles displayed decreased disease development and bacterial growth in response to R. solanacearum infection. We elucidated the underlying molecular mechanism by analyzing PRN 2 interactions with the papain‐like cysteine proteases ( PLCP s) XCP 2, RD 21A, and RD 21B, all of which bound to PRN 2 in yeast two‐hybrid assays and in Arabidopsis protoplast co‐immunoprecipitation assays. We show that XCP 2 is stabilized by PRN 2 through inhibition of its autolysis on the basis of PLCP activity profiling assays and enzymatic assays with recombinant protein. The stabilization of XCP 2 by PRN 2 was also confirmed in planta . Like prn2 mutants, an xcp2 single knockout mutant and xcp2 prn2 double knockout mutant displayed decreased susceptibility to R. solanacearum , suggesting that stabilization of XCP 2 by PRN 2 underlies susceptibility to R. solanacearum in Arabidopsis.