Document Detail

Elicitor-mediated oligomerization of the tobacco N disease resistance protein.
MedLine Citation:
PMID:  16387833     Owner:  NLM     Status:  MEDLINE    
Plant nucleotide binding site-leucine-rich repeat (NBS-LRR) proteins are similar to the nucleotide binding oligomerization domain (NOD) protein family in their domain structure. It has been suggested that most NOD proteins rely on ligand-mediated oligomerization for function, and we have tested this possibility with the N protein of tobacco (Nicotiana tabacum). The N gene for resistance to Tobacco mosaic virus (TMV) is a member of the Toll-interleukin receptor (TIR)-NBS-LRR class of plant disease resistance (R) genes that recognizes the helicase domain from the TMV replicase. Using transient expression followed by immunoprecipitation, we show that the N protein oligomerizes in the presence of the elicitor. The oligomerization was not affected by silencing Nicotiana benthamiana ENHANCED DISEASE SUSCEPTIBILITY1 and N REQUIREMENT GENE1 cofactors of N-mediated resistance, but it was abolished by a mutation in the P-loop motif. However, loss-of-function mutations in the RNBS-A motif and in the TIR domain retain the ability to oligomerize. From these results, we conclude that oligomerization is an early event in the N-mediated resistance to TMV.
Pere Mestre; David C Baulcombe
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2005-12-30
Journal Detail:
Title:  The Plant cell     Volume:  18     ISSN:  1040-4651     ISO Abbreviation:  Plant Cell     Publication Date:  2006 Feb 
Date Detail:
Created Date:  2006-02-02     Completed Date:  2006-08-04     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  9208688     Medline TA:  Plant Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  491-501     Citation Subset:  IM    
Sainsbury Laboratory, John Ines Centre, Norwich NR4 7UH, United Kingdom.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/AAA91022;  AAB47618;  AAC72977;  AAF08790;  AAR21295;  AF479625;  AF516180;  CAB50708;  DQ054580;  Q40392
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MeSH Terms
Amino Acid Motifs
Conserved Sequence
Gene Expression
Hemagglutinin Glycoproteins, Influenza Virus / metabolism
Immunity, Innate
Models, Biological
Molecular Sequence Data
Mutation / genetics
Peptide Fragments / metabolism
Plant Leaves / virology
Plant Proteins / chemistry*,  metabolism*
Protein Binding
Protein Structure, Quaternary
Sequence Alignment
Tobacco / anatomy & histology,  metabolism*,  virology
Tobacco Mosaic Virus / physiology
Toll-Like Receptors / chemistry,  metabolism
Reg. No./Substance:
0/Hemagglutinin Glycoproteins, Influenza Virus; 0/N protein, Nicotiana glutinosa; 0/Peptide Fragments; 0/Plant Proteins; 0/Toll-Like Receptors; 0/tyrosyl-prolyl-tyrosyl-aspartyl-valyl-prolyl-aspartyl-tyrosyl-alanine

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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