How to build a pathogen detector: structural basis of NB-LRR function

F.L.W. Takken; A. Goverse

doi:10.1016/j.pbi.2012.05.001

How to build a pathogen detector: structural basis of NB-LRR function

F.L.W. Takken
, A. Goverse

Laboratory of Nematology

Research output: Contribution to journal › Article › Academic › peer-review

250 Citations (Scopus)

Abstract

Many plant disease resistance (R) proteins belong to the family of nucleotide-binding-leucine rich repeat (NB-LRR) proteins. NB-LRRs mediate recognition of pathogen-derived effector molecules and subsequently activate host defence. Their multi-domain structure allows these pathogen detectors to simultaneously act as sensor, switch and response factor. Structure–function analyses and the recent elucidation of the 3D structures of subdomains have provided new insight in how these different functions are combined and what the contribution is of the individual subdomains. Besides interdomain contacts, interactions with chaperones, the proteasome and effector baits are required to keep NB-LRRs in a signalling-competent, yet auto-inhibited state. In this review we explore operational models of NB-LRR functioning based on recent advances in understanding their structure

Original language	English
Pages (from-to)	375-384
Journal	Current Opinion in Plant Biology
Volume	15
Issue number	4
DOIs	https://doi.org/10.1016/j.pbi.2012.05.001
Publication status	Published - 2012

Keywords

disease resistance protein
tobacco-mosaic-virus
rich repeat protein
c-terminal domain
cell-death
coiled-coil
flax rust
effector recognition
crystal-structure
arabidopsis eds1

Access to Document

10.1016/j.pbi.2012.05.001

Cite this

@article{e858c66621304b1ca0c2a08cf7752fef,

title = "How to build a pathogen detector: structural basis of NB-LRR function",

abstract = "Many plant disease resistance (R) proteins belong to the family of nucleotide-binding-leucine rich repeat (NB-LRR) proteins. NB-LRRs mediate recognition of pathogen-derived effector molecules and subsequently activate host defence. Their multi-domain structure allows these pathogen detectors to simultaneously act as sensor, switch and response factor. Structure–function analyses and the recent elucidation of the 3D structures of subdomains have provided new insight in how these different functions are combined and what the contribution is of the individual subdomains. Besides interdomain contacts, interactions with chaperones, the proteasome and effector baits are required to keep NB-LRRs in a signalling-competent, yet auto-inhibited state. In this review we explore operational models of NB-LRR functioning based on recent advances in understanding their structure",

keywords = "disease resistance protein, tobacco-mosaic-virus, rich repeat protein, c-terminal domain, cell-death, coiled-coil, flax rust, effector recognition, crystal-structure, arabidopsis eds1",

author = "F.L.W. Takken and A. Goverse",

year = "2012",

doi = "10.1016/j.pbi.2012.05.001",

language = "English",

volume = "15",

pages = "375--384",

journal = "Current Opinion in Plant Biology",

issn = "1369-5266",

publisher = "Elsevier",

number = "4",

}

TY - JOUR

T1 - How to build a pathogen detector: structural basis of NB-LRR function

AU - Takken, F.L.W.

AU - Goverse, A.

PY - 2012

Y1 - 2012

N2 - Many plant disease resistance (R) proteins belong to the family of nucleotide-binding-leucine rich repeat (NB-LRR) proteins. NB-LRRs mediate recognition of pathogen-derived effector molecules and subsequently activate host defence. Their multi-domain structure allows these pathogen detectors to simultaneously act as sensor, switch and response factor. Structure–function analyses and the recent elucidation of the 3D structures of subdomains have provided new insight in how these different functions are combined and what the contribution is of the individual subdomains. Besides interdomain contacts, interactions with chaperones, the proteasome and effector baits are required to keep NB-LRRs in a signalling-competent, yet auto-inhibited state. In this review we explore operational models of NB-LRR functioning based on recent advances in understanding their structure

AB - Many plant disease resistance (R) proteins belong to the family of nucleotide-binding-leucine rich repeat (NB-LRR) proteins. NB-LRRs mediate recognition of pathogen-derived effector molecules and subsequently activate host defence. Their multi-domain structure allows these pathogen detectors to simultaneously act as sensor, switch and response factor. Structure–function analyses and the recent elucidation of the 3D structures of subdomains have provided new insight in how these different functions are combined and what the contribution is of the individual subdomains. Besides interdomain contacts, interactions with chaperones, the proteasome and effector baits are required to keep NB-LRRs in a signalling-competent, yet auto-inhibited state. In this review we explore operational models of NB-LRR functioning based on recent advances in understanding their structure

KW - disease resistance protein

KW - tobacco-mosaic-virus

KW - rich repeat protein

KW - c-terminal domain

KW - cell-death

KW - coiled-coil

KW - flax rust

KW - effector recognition

KW - crystal-structure

KW - arabidopsis eds1

U2 - 10.1016/j.pbi.2012.05.001

DO - 10.1016/j.pbi.2012.05.001

M3 - Article

SN - 1369-5266

VL - 15

SP - 375

EP - 384

JO - Current Opinion in Plant Biology

JF - Current Opinion in Plant Biology

IS - 4

ER -

How to build a pathogen detector: structural basis of NB-LRR function

Abstract

Keywords

Access to Document

Fingerprint

Cite this