English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Zendy Plus

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Zendy Tools

Zendy Open

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.

PIRIN 2 stabilizes cysteine protease XCP 2 and increases susceptibility to the vascular pathogen Ralstonia solanacearum in Arabidopsis