title: AvrBsT acetylates Arabidopsis ACIP1, a protein that associates with microtubules and is required for immunity.
abstract: Bacterial pathogens of plant and animals share a homologous group of virulence factors, referred to as the YopJ effector family, which are translocated by the type III secretion (T3S) system into host cells during infection. Recent work indicates that some of these effectors encode acetyltransferases that suppress host immunity. The YopJ-like protein AvrBsT is known to activate effector-triggered immunity (ETI) in Arabidopsis thaliana Pi-0 plants; however, the nature of its enzymatic activity and host target(s) has remained elusive. Here we report that AvrBsT possesses acetyltransferase activity and acetylates ACIP1 (for ACETYLATED INTERACTING PROTEIN1), an unknown protein from Arabidopsis. Genetic studies revealed that Arabidopsis ACIP family members are required for both pathogen-associated molecular pattern (PAMP)-triggered immunity and AvrBsT-triggered ETI during Pseudomonas syringae pathovar tomato DC3000 (Pst DC3000) infection. Microscopy studies revealed that ACIP1 is associated with punctae on the cell cortex and some of these punctae co-localize with microtubules. These structures were dramatically altered during infection. Pst DC3000 or Pst DC3000 AvrRpt2 infection triggered the formation of numerous, small ACIP1 punctae and rods. By contrast, Pst DC3000 AvrBsT infection primarily triggered the formation of large GFP-ACIP1 aggregates, in an acetyltransferase-dependent manner. Our data reveal that members of the ACIP family are new components of the defense machinery required for anti-bacterial immunity. They also suggest that AvrBsT-dependent acetylation in planta alters ACIP1's defense function, which is linked to the activation of ETI.
authors.affiliation: Department of Biology, Stanford University, Stanford, California, United States of America.
authors.forename: Mi Sun
authors.initials: MS
authors.lastname: Cheong
authors.affiliation: School of Biological Sciences, Illinois State University, Normal, Illinois, United States of America.
authors.forename: Angela
authors.initials: A
authors.lastname: Kirik
authors.affiliation: Department of Biology, Stanford University, Stanford, California, United States of America.
authors.forename: Jung-Gun
authors.initials: JG
authors.lastname: Kim
authors.affiliation: Department of Biology, Stanford University, Stanford, California, United States of America.
authors.forename: Kenneth
authors.initials: K
authors.lastname: Frame
authors.affiliation: School of Biological Sciences, Illinois State University, Normal, Illinois, United States of America.
authors.forename: Viktor
authors.initials: V
authors.lastname: Kirik
authors.affiliation: Department of Biology, Stanford University, Stanford, California, United States of America.
authors.forename: Mary Beth
authors.initials: MB
authors.lastname: Mudgett
mesh_terms: D000107:Acetylation; D017360:Arabidopsis / Q000378:metabolism* / Q000382:microbiology*; D029681:Arabidopsis Proteins / Q000378:metabolism*; D008870:Microtubules / Q000378:metabolism; D010935:Plant Diseases / Q000382:microbiology; D030821:Plants, Genetically Modified; D016133:Polymerase Chain Reaction; D011552:Pseudomonas Infections / Q000378:metabolism*; D044224:Pseudomonas syringae / Q000472:pathogenicity*; D020798:Two-Hybrid System Techniques; D037521:Virulence Factors / Q000378:metabolism
chemical_list: D029681:Arabidopsis Proteins; D037521:Virulence Factors