Diversity of Serine Hydrolase Activities of Unchallenged and Botrytis-infected Arabidopsis thaliana

Activity-based protein profiling is a powerful method to display enzyme activities in proteomes and provides crucial information on enzyme activity rather than protein or transcript abundance. We applied activity-based protein profiling using fluorophosphonate-based probes to display the activities...

Full description

Saved in:
Bibliographic Details
Published in:Molecular & cellular proteomics 2009-05, Vol.8 (5), p.1082-1093
Main Authors: Kaschani, Farnusch, Gu, Christian, Niessen, Sherry, Hoover, Heather, Cravatt, Benjamin F, van der Hoorn, Renier A L
Format: Article
Language:English
Subjects:
Acyltransferases - metabolism
Agrobacterium tumefaciens
Amino Acid Sequence
Arabidopsis - enzymology
Arabidopsis - microbiology
Arabidopsis Proteins - metabolism
Botrytis - physiology
Host-Pathogen Interactions
Molecular Sequence Data
Nicotiana - metabolism
Organophosphonates - metabolism
Peptides - chemistry
Plant Leaves - enzymology
Plant Leaves - microbiology
Serine Endopeptidases - analysis
Serine Endopeptidases - metabolism
Tissue Extracts
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Activity-based protein profiling is a powerful method to display enzyme activities in proteomes and provides crucial information on enzyme activity rather than protein or transcript abundance. We applied activity-based protein profiling using fluorophosphonate-based probes to display the activities of Ser hydrolases in the model plant Arabidopsis thaliana . Multidimensional protein identification technology and in-gel analysis of fluorophosphonate-labeled leaf extracts revealed over 50 Ser hydrolases, including dozens of proteases, esterases, and lipases, representing over 10 different enzyme families. Except for some well characterized Ser hydrolases like subtilases TPP2 and ARA12, prolyl oligopeptidase acylamino acid-releasing enzyme, serine carboxypeptidase-like SNG1 and BRS1, carboxylesterase-like CXE12, methylesterases MES2 and MES3, and S -formylglutathione hydrolase, the majority of these serine hydrolases have not been described before. We studied transiently expressed SNG1 and investigated plants infected with the fungal pathogen Botrytis cinerea . Besides the down-regulation of several Arabidopsis Ser hydrolase activities during Botrytis infection, we detected the activities of Botrytis -derived cutinases and lipases, which are thought to contribute to pathogenicity.
ISSN:1535-9476
1535-9484
DOI:10.1074/mcp.M800494-MCP200