Premium
Activity profiling of vacuolar processing enzymes reveals a role for VPE during oomycete infection
Author(s) -
MisasVillamil Johana C.,
Toenges Gerrit,
Kolodziejek Izabella,
Sadaghiani Amir M.,
Kaschani Farnusch,
Colby Thomas,
Bogyo Matthew,
Hoorn Renier A.L.
Publication year - 2013
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.12062
Subject(s) - oomycete , proteases , microbiology and biotechnology , biology , mutant , enzyme , cysteine , programmed cell death , obligate , in vivo , pathogen , biochemistry , apoptosis , botany , gene , genetics
Summary Vacuolar processing enzymes ( VPE s) are important cysteine proteases that are implicated in the maturation of seed storage proteins, and programmed cell death during plant–microbe interactions and development. Here, we introduce a specific, cell‐permeable, activity‐based probe for VPE s. This probe is highly specific for all four A rabidopsis VPE s, and labeling is activity‐dependent, as illustrated by sensitivity for inhibitors, pH and reducing agents. We show that the probe can be used for in vivo imaging and displays multiple active isoforms of VPE s in various tissues and in both monocot and dicot plant species. Thus, VPE activity profiling is a robust, simple and powerful tool for plant research for a wide range of applications. Using VPE activity profiling, we discovered that VPE activity is increased during infection with the oomycete pathogen H yaloperonospora arabidopsidis ( Hpa ). The enhanced VPE activity is host‐derived and EDS1 ‐independent. Sporulation of Hpa is reduced on vpe mutant plants, demonstrating a role for VPE during compatible interactions that is presumably independent of programmed cell death. Our data indicate that, as an obligate biotroph, Hpa takes advantage of increased VPE activity in the host, e.g. to mediate protein turnover and nutrient release.