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  Resistance proteins: molecular switches of plant defence

Takken, F. L., Albrecht, M., & Tameling, W. I. (2006). Resistance proteins: molecular switches of plant defence. Current Opinion in Plant Biology, 9, 383-390.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-000F-23DE-2 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-000F-23DF-F
Genre: Journal Article

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 Creators:
Takken, Frank L., Author
Albrecht, Mario1, Author           
Tameling, Wladimir I., Author
Affiliations:
1Computational Biology and Applied Algorithmics, MPI for Informatics, Max Planck Society, ou_40046              

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 Abstract: Specificity of the plant innate immune system is often conferred by resistance (R) proteins. Most R proteins contain leucine-rich repeats (LRRs), a central nucleotide-binding site (NBS) and a variable amino-terminal domain. The LRRs are mainly involved in recognition, whereas the amino-terminal domain determines signalling specificity. The NBS forms part of a nucleotide binding (NB)-ARC domain that presumably functions as a molecular switch. The conserved nature of NB-ARC proteins makes it possible to map mutations of R protein residues onto the crystal structures of related NB-ARC proteins, providing hypotheses for the functional roles of these residues. A functional model emerges in which the LRRs control the molecular state of the NB-ARC domain. Pathogen recognition triggers nucleotide-dependent conformational changes that might induce oligomerisation, thereby providing a scaffold for activation of downstream signalling components.

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Language(s): eng - English
 Dates: 2007-02-222006
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 314505
Other: Local-ID: C125673F004B2D7B-8EB4E2D106B8DB00C125713A0066CB86-Albrecht2006c
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Title: Current Opinion in Plant Biology
Source Genre: Journal
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Pages: - Volume / Issue: 9 Sequence Number: - Start / End Page: 383 - 390 Identifier: -