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Title: A hydrophobic anchor mechanism defines a deacetylase family that suppresses host response against YopJ effectors

Journal Article · · Nature Communications
ORCiD logo [1];  [1];  [2]
  1. Salk Institute for Biological Studies,La Jolla, CA, (United States). Plant Biology Laboratory
  2. Salk Institute for Biological Studies, La Jolla, CA, (United States). Plant Biology Laboratory; Salk Institute for Biological Studies, La Jolla, CA, (United States). Howard Hughes Medical Institute

Several Pseudomonas<\em> and Xanthomonas<\em> species are plant pathogens that infect the model organism Arabidopsis<\em> thaliana<\em> and important crops such as Brassica<\em>. Resistant plants contain the infection by rapid cell death of the infected area through the hypersensitive response (HR). A family of highly related α/β hydrolases is involved in diverse processes in all domains of life. Functional details of their catalytic machinery, however, remained unclear. We report the crystal structures of α/β hydrolases representing two different clades of the family, including the protein SOBER1, which suppresses AvrBsT-incited HR in Arabidopsis<\em>. Our results reveal a unique hydrophobic anchor mechanism that defines a previously unknown family of protein deacetylases. Furthermore, this study identifies a lid-loop as general feature for substrate turnover in acyl-protein thioesterases and the described family of deacetylases. Furthermore, we found that SOBER1’s biological function is not restricted to Arabidopsis<\em> thaliana<\em> and not limited to suppress HR induced by AvrBsT.

Research Organization:
Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES)
Grant/Contract Number:
AC02-05CH11231
OSTI ID:
1624065
Journal Information:
Nature Communications, Vol. 8, Issue 1; ISSN 2041-1723
Publisher:
Nature Publishing GroupCopyright Statement
Country of Publication:
United States
Language:
English

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