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  The cf-9 disease resistance protein is present in an similar to 420-kilodalton heteromultimeric membrane-associated complex at one molecule per complex

Rivas, S., Romeis, T., & Jones, J. D. G. (2002). The cf-9 disease resistance protein is present in an similar to 420-kilodalton heteromultimeric membrane-associated complex at one molecule per complex. Plant Cell, 14(3), 689-702.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-3E02-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-3E03-3
Genre: Journal Article

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Rivas, S., Author
Romeis, T.1, Author              
Jones, J. D. G., Author
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1Dept. of Plant Microbe Interactions (Paul Schulze-Lefert), MPI for Plant Breeding Research, Max Planck Society, ou_1113572              

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 Abstract: The tomato Cf-9 gene confers race-specific resistance to the fungal pathogen Cladosporium fulvum expressing the corresponding avirulence gene Avr9. In tobacco, Cf-9 confers a hypersensitive response to the Avr9 peptide. To investigate Cf- 9 protein function in initiating defense signaling, we engineered a functional C-terminal fusion of the Cf-9 gene with the TAP (Tandem Affinity Purification) tag. In addition, we established a transient expression assay in Nicotiana benthamiana leaves for the production of functional Cf-9:myc and Cf-9:TAP. Transiently expressed Cf-9:myc and Cf-9:TAP proteins induced an Avr9-dependent hypersensitive response, consistent with previous results with stably transformed tobacco plants and derived cell suspension cultures expressing c-myc-tagged Cf-9. Gel filtration of microsomal fractions solubilized with octylglucoside revealed that the Cf-9 protein, either as c-myc or TAP fusions, migrated at a molecular mass of 350 to 475 kD. By using blue native gel electrophoresis, the molecular size was confirmed to be similar to420 kD. Our results suggest that only one Cf-9 protein molecule is present in the Cf-9 complex and that Cf-9 is part of a membrane complex consisting of an additional glycoprotein partner(s). The high structural similarity between Cf proteins and Clavata2 (CLV2) of Arabidopsis, together with the similarity of molecular mass between Cf-9 and CLV complexes (420 and 450 kD, respectively), led us to investigate whether Cf-9 is integrated into membrane- associated protein complexes like those formed by CLV1 and CLV2. Unlike CLV2, the Cf-9 protein did not form disulfide- linked heterodimers, no ligand (Avr9)-dependent shift in the molecular mass of the Cf-9 complex was detected, and no Rho- GTPase-related proteins were found associated with Cf-9 under the conditions tested. Thus, Cf-9-dependent defense signaling and CLV2-dependent regulation of meristem development seem to be accomplished via distinct mechanisms, despite the structural similarity of their key components Cf-9 and CLV2.

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Language(s): eng - English
 Dates: 2002-03
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: eDoc: 28818
ISI: 000174788700015
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Title: Plant Cell
  Alternative Title : Plant Cell
Source Genre: Journal
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Pages: - Volume / Issue: 14 (3) Sequence Number: - Start / End Page: 689 - 702 Identifier: ISSN: 1040-4651