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

Abstract:

:Proteins with a CyaB, thiamine triphosphatase domain (CYTH domain) may play a central role at the interface between nucleotide and polyphosphate metabolism. One of the plant CYTH domain-containing proteins from Brachypodium distachyon, BdTTM3, is annotated in NCBI databases as an 'adenylyl cyclase (AC)' or a 'triphosphate tunnel metalloenzyme'. The divergent nomenclature and the search for plant ACs induced us to experimentally confirm the enzymatic activity of BdTTM3. Based on in vitro analysis, we have shown that the recombinant form of BdTTM3 is a protein with high triphosphatase activity (binding both tripolyphosphate and ATP) and low AC activity. Furthermore, the analysis of BdTTM3 transcriptional activity indicates its involvement in the mechanism underlying responses to wounding stress in B. distachyon leaves.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Świeżawska B,Duszyn M,Kwiatkowski M,Jaworski K,Pawełek A,Szmidt-Jaworska A

doi

10.1002/1873-3468.13701

subject

Has Abstract

pub_date

2020-03-01 00:00:00

pages

1101-1111

issue

6

eissn

0014-5793

issn

1873-3468

journal_volume

594

pub_type

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