Catalase, glutathione and protein phosphatase 2A-dependent organellar redox signalling regulate aphid fecundity under moderate and high irradiance.

07:00 EST 8th November 2019 | BioPortfolio

Summary of "Catalase, glutathione and protein phosphatase 2A-dependent organellar redox signalling regulate aphid fecundity under moderate and high irradiance."

Redox processes regulate plant/insect responses but the precise roles of environmental triggers and specific molecular components remain poorly defined. Aphid fecundity and plant responses were therefore measured in Arabidopsis thaliana mutants deficient in either catalase 2 (cat2), different protein phosphatase 2A (PP2A) subunits or glutathione (cad2, pad2, clt1) under either moderate (250 μmol m s ) or high (800 μmol m s ) light. Aphid fecundity was decreased in pp2a-b'γ, cat2 and the cat2 pp2a-b'γ double mutants relative to the wild type under moderate irradiance. High light decreased aphid numbers in all genotypes except for cat2. Aphid fecundity was similar in the cat2 and glutathione-, phytoalexin- and glucosinolate-deficient cat2cad2 double mutants under both irradiances. Aphid-induced increases in transcripts encoding the abscisic acid-related ARABIDOPSIS ZINC-FINGER PROTEIN 1 (AZF1) transcription factor were observed only under moderate light. Conversely, aphid induced increases in transcripts encoding the jasmonate-synthesis enzyme ALLENE OXIDE CYCLASE 3 (AOC3) was observed in all genotypes only under high light. Aphid-induced increases in REDOX RESPONSIVE TRANSCRIPTION FACTOR 1 (RRTF1) mRNAs were observed in all genotypes except pp2a-b'ζ1-1 under both irradiances. Aphid fecundity is therefore regulated by cellular redox signalling that is mediated, at least in part, through PP2A-dependent mitochondria to nucleus signalling pathways.


Journal Details

This article was published in the following journal.

Name: Plant, cell & environment
ISSN: 1365-3040


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Medical and Biotech [MESH] Definitions

A glutathione transferase that catalyzes the conjugation of electrophilic substrates to GLUTATHIONE. This enzyme has been shown to provide cellular protection against redox-mediated damage by FREE RADICALS.

One of four major classes of mammalian serine/threonine specific protein phosphatases. Protein phosphatase 2C is a monomeric enzyme about 42 kDa in size. It shows broad substrate specificity dependent on divalent cations (mainly manganese and magnesium). Three isozymes are known in mammals: PP2C -alpha, -beta and -gamma. In yeast, there are four PP2C homologues: phosphatase PTC1 that have weak tyrosine phosphatase activity, phosphatase PTC2, phosphatase PTC3, and PTC4. Isozymes of PP2C also occur in Arabidopsis thaliana where the kinase-associated protein phosphatase (KAPP) containing a C-terminal PP2C domain, dephosphorylates Ser/Thr receptor-like kinase RLK5.

A subtype of non-receptor protein tyrosine phosphatase that is closely-related to PROTEIN TYROSINE PHOSPHATASE, NON-RECEPTOR TYPE 1. Alternative splicing of the mRNA for this phosphatase results in the production at two gene products, one of which includes a C-terminal nuclear localization domain that may be involved in the transport of the protein to the CELL NUCLEUS. Although initially referred to as T-cell protein tyrosine phosphatase the expression of this subtype occurs widely.

An enzyme that catalyzes the reduction of a protein-disulfide in the presence of glutathione, forming a protein-dithiol. Insulin is one of its substrates. EC

A phosphoprotein phosphatase subtype that is comprised of a catalytic subunit and two different regulatory subunits. At least two genes encode isoforms of the protein phosphatase catalytic subunit, while several isoforms of regulatory subunits exist due to the presence of multiple genes and the alternative splicing of their mRNAs. Protein phosphatase 2 acts on a broad variety of cellular proteins and may play a role as a regulator of intracellular signaling processes.

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