Evidence map›Paper›PMID 16489136›Full record

ArticlePlant physiology2006

Mutations in the NB-ARC domain of I-2 that impair ATP hydrolysis cause autoactivation.

Wladimir I L Tameling, Jack H Vossen, Mario Albrecht, Thomas Lengauer, Jan A Berden, Michel A Haring, Ben J C Cornelissen, Frank L W Takken

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 130 papers.

0numbers the graph read from it
0cells of the map it votes in
130citing papers in PubMed
22.4field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

130 citing papers in PubMed, 311 citations in OpenAlex.

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  11. Identification and Functional Analysis of thePlants (Basel, Switzerland) · 2024
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  15. Fine mapping and identification of a Fusarium wilt resistance gene FwS1 in pea.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2024
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  18. NLR- andPlants (Basel, Switzerland) · 2023
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  20. Review

70 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

Wladimir I L TamelingPlant Pathology, Swammerdam Institute for Life Sciences, University of Amsterdam, 1090 GB Amsterdam, The Netherlands.
Jack H Vossen
Mario Albrecht
Thomas Lengauer
Jan A Berden
Michel A Haring
Ben J C Cornelissen
Frank L W Takken
Max Planck Institute for Informatics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Resistance (R) proteins in plants confer specificity to the innate immune system. Most R proteins have a centrally located NB-ARC (nucleotide-binding adaptor shared by APAF-1, R proteins, and CED-4) domain. For two tomato (Lycopersicon esculentum) R proteins, I-2 and Mi-1, we have previously shown that this domain acts as an ATPase module that can hydrolyze ATP in vitro. To investigate the role of nucleotide binding and hydrolysis for the function of I-2 in planta, specific mutations were introduced in conserved motifs of the NB-ARC domain. Two mutations resulted in autoactivating proteins that induce a pathogen-independent hypersensitive response upon expression in planta. These mutant forms of I-2 were found to be impaired in ATP hydrolysis, but not in ATP binding, suggesting that the ATP- rather than the ADP-bound state of I-2 is the active form that triggers defense signaling. In addition, upon ADP binding, the protein displayed an increased affinity for ADP suggestive of a change of conformation. Based on these data, we propose that the NB-ARC domain of I-2, and likely of related R proteins, functions as a molecular switch whose state (on/off) depends on the nucleotide bound (ATP/ADP).

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateAmino Acid MotifsAmino Acid SequenceGene Expression Regulation, PlantHydrolysisModels, BiologicalModels, MolecularMolecular Sequence DataPlant LeavesPlant ProteinsPoint MutationProtein Structure, TertiarySequence AlignmentSolanum lycopersicumAdenosine TriphosphatasesAdenosine TriphosphatePlant Proteins

Identifiers

PMID16489136
PMCPMC1459841
OpenAlexW1993339029

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.