<i>Brachypodium distachyon</i> triphosphate tunnel metalloenzyme 3 is both a triphosphatase and an adenylyl cyclase upregulated by mechanical wounding

Świeżawska, Brygida; Duszyn, Maria; Kwiatkowski, Mateusz; Jaworski, Krzysztof; Pawełek, Agnieszka; Szmidt-Jaworska, Adriana

doi:10.1002/1873-3468.13701

Cited by 15 publications

(16 citation statements)

References 37 publications

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“…The Arabidopsis TTM3 ( At TTM3) knockout plant showed an anomalous root phenotype, indicating a potential role in root development ( 22 ). Although it has been established that plant TTMs act as a polyphosphate hydrolase, recent reports suggest that Brachypodium distachyon and Hippeastrum x hybridum TTM proteins might be able to produce a low amount of cAMP under laboratory conditions ( 23 , 24 ). In our enzyme function–based cluster analysis ( Fig.…”

Section: Discussionmentioning

confidence: 99%

The archaeal triphosphate tunnel metalloenzyme SaTTM defines structural determinants for the diverse activities in the CYTH protein family

Vogt

Nguepbeu

Mohr

et al. 2021

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

The archaeal triphosphate tunnel metalloenzyme SaTTM defines structural determinants for the diverse activities in the CYTH protein family

Vogt

Nguepbeu

Mohr

et al. 2021

Journal of Biological Chemistry

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“…Although a causal relationship was not demonstrated, HpGC1 activity may relate to downstream production of cGMP in the challenged scales ( Świeżawska et al, 2015 ). Since then, triphosphate tunnel metalloenzyme 3 (TTM3) from Brachypodium distachyon has been found to have both ATP hydrolyzing and AC activities, with upregulation of transcription by wounding ( Świeżawska et al, 2019 ). There remains a significant knowledge gap when it comes to whether eATP as a DAMP (or in its role as growth regulator) has an effect on cAMP or cGMP levels.…”

Section: Cyclic Nucleotide Production By Moonlighting Proteins In Response To Pathogens and Woundingmentioning

confidence: 99%

Damage Signaling by Extracellular Nucleotides: A Role for Cyclic Nucleotides in Elevating Cytosolic Free Calcium?

et al. 2021

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Extracellular ATP (eATP) is now held to be a constitutive damage-associated molecular pattern (DAMP) that is released by wounding, herbivory or pathogen attack. The concentration of eATP must be tightly regulated as either depletion or overload leads to cell death. In Arabidopsis thaliana, sensing of eATP is by two plasma membrane legume-like lectin serine–threonine receptor kinases (P2K1 and P2K2), although other receptors are postulated. The transcriptional response to eATP is dominated by wound- and defense-response genes. Wounding and pathogen attack can involve the cyclic nucleotides cyclic AMP (cAMP) and cyclic GMP (cGMP) which, in common with eATP, can increase cytosolic-free Ca2+ as a second messenger. This perspective on DAMP signaling by eATP considers the possibility that the eATP pathway involves production of cyclic nucleotides to promote opening of cyclic nucleotide-gated channels and so elevates cytosolic-free Ca2+. In silico analysis of P2K1 and P2K2 reveals putative adenylyl and guanylyl kinase sequences that are the hallmarks of “moonlighting” receptors capable of cAMP and cGMP production. Further, an Arabidopsis loss of function cngc mutant was found to have an impaired increase in cytosolic-free Ca2+ in response to eATP. A link between eATP, cyclic nucleotides, and Ca2+ signaling therefore appears credible.

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“…The picture that emerges is that TTM proteins evolved from an inorganic tripolyphosphatase acquiring new substrate specificities in fungi and some protists (RNA triphosphatase) and animals (ThTPase) or even new catalytic mechanisms in some bacteria (CyaB like adenylyl cyclase) [ 83 ]. The recombinant form of the plant Brachypodium distachyon (BdTTM3) even shares high triphosphatase activity (binding both tripolyphosphate and ATP) and low adenylate cyclase activity and might be involved in the mechanism underlying responses to wounding stress [ 84 ].…”

Section: Thiamine Triphosphatasesmentioning

confidence: 99%

“…Lately, pyrophosphatase activity (PPase) was recognized in A. thaliana TTM1 and TTM2, proteins containing a TTM and a uridine kinase domain [ 87 ]. The plant B. distachyon (BdTTM3) shares high triphosphatase activity and low adenylyl cyclase activity [ 84 ]. We hypothesize that the original activity in the Last Universal Common Ancestor (LUCA) was the hydrolysis of low molecular mass polyphosphates.…”

Section: Thiamine Triphosphatasesmentioning

confidence: 99%

Update on Thiamine Triphosphorylated Derivatives and Metabolizing Enzymatic Complexes

Bettendorff

2021

Biomolecules

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While the cellular functions of the coenzyme thiamine (vitamin B1) diphosphate (ThDP) are well characterized, the triphosphorylated thiamine derivatives, thiamine triphosphate (ThTP) and adenosine thiamine triphosphate (AThTP), still represent an intriguing mystery. They are present, generally in small amounts, in nearly all organisms, bacteria, fungi, plants, and animals. The synthesis of ThTP seems to require ATP synthase by a mechanism similar to ATP synthesis. In E. coli, ThTP is synthesized during amino acid starvation, while in plants, its synthesis is dependent on photosynthetic processes. In E. coli, ThTP synthesis probably requires oxidation of pyruvate and may play a role at the interface between energy and amino acid metabolism. In animal cells, no mechanism of regulation is known. Cytosolic ThTP levels are controlled by a highly specific cytosolic thiamine triphosphatase (ThTPase), coded by thtpa, and belonging to the ubiquitous family of the triphosphate tunnel metalloenzymes (TTMs). While members of this protein family are found in nearly all living organisms, where they bind organic and inorganic triphosphates, ThTPase activity seems to be restricted to animals. In mammals, THTPA is ubiquitously expressed with probable post-transcriptional regulation. Much less is known about the recently discovered AThTP. In E. coli, AThTP is synthesized by a high molecular weight protein complex from ThDP and ATP or ADP in response to energy stress. A better understanding of these two thiamine derivatives will require the use of transgenic models.

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Brachypodium distachyon triphosphate tunnel metalloenzyme 3 is both a triphosphatase and an adenylyl cyclase upregulated by mechanical wounding

Cited by 15 publications

References 37 publications

The archaeal triphosphate tunnel metalloenzyme SaTTM defines structural determinants for the diverse activities in the CYTH protein family

The archaeal triphosphate tunnel metalloenzyme SaTTM defines structural determinants for the diverse activities in the CYTH protein family

Damage Signaling by Extracellular Nucleotides: A Role for Cyclic Nucleotides in Elevating Cytosolic Free Calcium?

Update on Thiamine Triphosphorylated Derivatives and Metabolizing Enzymatic Complexes

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