Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2011-4-4
pubmed:abstractText
Numerous fungal and oomycete pathogens penetrate the plant cell wall and extract nutrition from the host cells by a feeding structure called the haustorium. We recently revealed that the Arabidopsis resistance protein RPW8.2 is specifically targeted to the extrahaustorial membrane (EHM) for activation of haustorium-targeted resistance to powdery mildew pathogens. Consistent with its EHM-localization, RPW8.2 contains a putative transmembrane (TM) domain at its N-terminus. Here, we show that translational fusion of YFP to the N-terminus of RPW8.2 results in localization of YFP-RPW8.2 to both the plasma membrane and the EHM, and loss of RPW8.2's defense function. We also show that deletion of the TM domain results in mis-localization of the RPW8.2-YFP fusion protein and extremely low levels of accumulation. These results indicate that an intact N-terminal TM domain is necessary for EHM-specific localization and defense function of RPW8.2. In addition, we show that when expressed from the strong constitutive 35S viral promoter, RPW8.2 accumulates at low levels in the EHM insufficient to activate resistance, highlighting the importance of stronger spatiotemporal expression of RPW8.2 from its native promoter. Taken together, our results indicate that accurate and adequate spatiotemporal expression and localization of RPW8.2 is key to activation of resistance at the host-pathogen interface.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1559-2324
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1002-5
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Accurate and adequate spatiotemporal expression and localization of RPW8.2 is key to activation of resistance at the host-pathogen interface.
pubmed:affiliation
Institute for Bioscience and Biotechnology Research, University of Maryland, Shady Grove, Maryland, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.