Publication Date:
2000-11-25
Description:
Homologs of the Yersinia virulence effector YopJ are found in both plant and animal bacterial pathogens, as well as plant symbionts. These YopJ family members were shown to act as cysteine proteases. The catalytic triad of the protease was required for inhibition of the mitogen-activated protein kinase (MAPK) and nuclear factor kappaB (NF-kappaB) signaling in animal cells and for induction of localized cell death in plants. The substrates for YopJ were shown to be highly conserved ubiquitin-like molecules, which are covalently added to numerous regulatory proteins. YopJ family members exert their pathogenic effect on cells by disrupting this posttranslational modification.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Orth, K -- Xu, Z -- Mudgett, M B -- Bao, Z Q -- Palmer, L E -- Bliska, J B -- Mangel, W F -- Staskawicz, B -- Dixon, J E -- 18024/PHS HHS/ -- AI41599/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2000 Nov 24;290(5496):1594-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109-0606, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11090361" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Animals
;
Bacterial Proteins/*chemistry/genetics/*metabolism
;
Catalysis
;
Catalytic Domain
;
Cell Line
;
Cysteine Endopeptidases/chemistry/genetics/*metabolism
;
Humans
;
*MAP Kinase Signaling System
;
Mitogen-Activated Protein Kinases/metabolism
;
Molecular Sequence Data
;
NF-kappa B/*metabolism
;
Plant Leaves/cytology/virology
;
SUMO-1 Protein
;
Sequence Alignment
;
Signal Transduction
;
Transfection
;
Ubiquitins/metabolism
;
Virulence
;
Xanthomonas campestris/enzymology/pathogenicity
;
Yersinia pseudotuberculosis/enzymology/metabolism/*pathogenicity
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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