ArticlePlant physiology2004
Poplar peroxiredoxin Q. A thioredoxin-linked chloroplast antioxidant functional in pathogen defense.
Article in Plant physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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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.
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Who cites it
56 citing papers in PubMed, 173 citations in OpenAlex.
- OsDUF2488 acts synergistically with OsPrx1.1, regulates ROS metabolism and promotes dehydration tolerance in rice.Plant biotechnology journal · 2025Article
- A fungal pathogen suppresses host leaf senescence to increase infection.Nature communications · 2025Article
- Identifying Endogenous Proteins of Perennial Ryegrass (Proteomes · 2025Article
- The Mechanisms Underlying Salt Resistance Mediated by Exogenous Application of 24-Epibrassinolide in Peanut.International journal of molecular sciences · 2022Article
- Thiol Reductases inAntioxidants (Basel, Switzerland) · 2022Review
- An improved and efficient method of Agrobacterium syringe infiltration for transient transformation and its application in the elucidation of gene function in poplar.BMC plant biology · 2021Article
- Redox regulation by peroxiredoxins is linked to their thioredoxin-dependent oxidase function.Photosynthesis research · 2020Article
- Chilli leaf curl virus infection downregulates the expression of the genes encoding chloroplast proteins and stress-related proteins.Physiology and molecular biology of plants : an international journal of functional plant biology · 2019Article
- Suppression of External NADPH Dehydrogenase-NDB1 inInternational journal of molecular sciences · 2018Article
- A thioredoxin-dependent peroxiredoxin Q from Corynebacterium glutamicum plays an important role in defense against oxidative stress.PloS one · 2018Article
- Article
- Proteomic analysis of Potentilla fruticosa L. leaves by iTRAQ reveals responses to heat stress.PloS one · 2017Article
- Peroxiredoxin Catalysis at Atomic Resolution.Structure (London, England : 1993) · 2016Article
- The Poplar Rust-Induced Secreted Protein (RISP) Inhibits the Growth of the Leaf Rust Pathogen Melampsora larici-populina and Triggers Cell Culture Alkalinisation.Frontiers in plant science · 2016Article
- The cold responsive mechanism of the paper mulberry: decreased photosynthesis capacity and increased starch accumulation.BMC genomics · 2015Article
- Peanut rust (Puccinia arachidis Speg.) disease: its background and recent accomplishments towards disease resistance breeding.Protoplasma · 2015Review
- The basics of thiols and cysteines in redox biology and chemistry.Free radical biology & medicine · 2015Review
- Article
- Chloroplastic thioredoxin-f and thioredoxin-m1/4 play important roles in brassinosteroids-induced changes in CO2 assimilation and cellular redox homeostasis in tomato.Journal of experimental botany · 2014Article
- In the absence of thioredoxins, what are the reductants for peroxiredoxins in Thermotoga maritima?Antioxidants & redox signaling · 2013Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peroxiredoxins are ubiquitous thioredoxin- or glutaredoxin-dependent peroxidases, the function of which is to destroy peroxides. Peroxiredoxin Q, one of the four plant subtypes, is a homolog of the bacterial bacterioferritin comigratory proteins. We show here that the poplar (Populus tremula x Populus tremuloides) protein acts as a monomer with an intramolecular disulfide bridge between two conserved cysteines. A wide range of electron donors and substrates was tested. Unlike type II peroxiredoxin, peroxiredoxin Q cannot use the glutaredoxin or cyclophilin isoforms tested, but various cytosolic, chloroplastic, and mitochondrial thioredoxins are efficient electron donors with no marked specificities. The redox midpoint potential of the peroxiredoxin Q catalytic disulfide is -325 mV at pH 7.0, explaining why the wild-type protein is reduced by thioredoxin but not by glutaredoxin. Additional evidence that thioredoxin serves as a donor comes from the formation of heterodimers between peroxiredoxin Q and monocysteinic mutants of spinach (Spinacia oleracea) thioredoxin m. Peroxiredoxin Q can reduce various alkyl hydroperoxides, but with a better efficiency for cumene hydroperoxide than hydrogen peroxide and tertiary butyl hydroperoxide. The use of immunolocalization and of a green fluorescence protein fusion construct indicates that the transit sequence efficiently targets peroxiredoxin Q to the chloroplasts and especially to those of the guard cells. The expression of this protein and of type II peroxiredoxin is modified in response to an infection by two races of Melampsora larici-populina, the causative agent of the poplar rust. In the case of an hypersensitive response, the peroxiredoxin expression increased, whereas it decreased during a compatible interaction.
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Registered trials
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.