Publication Date:
2009-05-09
Description:
Plant pathogenic bacteria secrete effector proteins that attack the host signaling machinery to suppress immunity. Effectors can be recognized by hosts leading to immunity. One such effector is AvrPtoB of Pseudomonas syringae, which degrades host protein kinases, such as tomato Fen, through an E3 ligase domain. Pto kinase, which is highly related to Fen, recognizes AvrPtoB in conjunction with the resistance protein Prf. Here we show that Pto is resistant to AvrPtoB-mediated degradation because it inactivates the E3 ligase domain. AvrPtoB ubiquitinated Fen within the catalytic cleft, leading to its breakdown and loss of the associated Prf protein. Pto avoids this by phosphorylating and inactivating the AvrPtoB E3 domain. Thus, inactivation of a pathogen virulence molecule is one mechanism by which plants resist disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ntoukakis, Vardis -- Mucyn, Tatiana S -- Gimenez-Ibanez, Selena -- Chapman, Helen C -- Gutierrez, Jose R -- Balmuth, Alexi L -- Jones, Alexandra M E -- Rathjen, John P -- BB/D00456X/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2009 May 8;324(5928):784-7. doi: 10.1126/science.1169430.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sainsbury Laboratory, Colney, Norwich NR4 7UH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19423826" target="_blank"〉PubMed〈/a〉
Keywords:
Bacterial Proteins/*antagonists & inhibitors/chemistry/genetics/metabolism
;
Immunity, Innate
;
Lycopersicon esculentum/genetics/*metabolism/*microbiology
;
Mutant Proteins/metabolism
;
Phosphorylation
;
Plant Diseases/immunology/*microbiology
;
Plant Leaves/metabolism
;
Plant Proteins/*metabolism
;
Plants, Genetically Modified
;
Protein Structure, Tertiary
;
Protein-Serine-Threonine Kinases/*metabolism
;
Pseudomonas syringae/genetics/growth & development/metabolism/*pathogenicity
;
Signal Transduction
;
Tobacco/genetics/metabolism/microbiology
;
Ubiquitin-Protein Ligases/metabolism
;
Ubiquitination
;
Virulence Factors/antagonists & inhibitors/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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