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Brachypodium distachyon triphosphate tunnel metalloenzyme 3 is both a triphosphatase and an adenylyl cyclase upregulated by mechanical wounding
Author(s) -
Świeżawska Brygida,
Duszyn Maria,
Kwiatkowski Mateusz,
Jaworski Krzysztof,
Pawełek Agnieszka,
SzmidtJaworska Adriana
Publication year - 2020
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13701
Subject(s) - brachypodium distachyon , biochemistry , adenylyl cyclase , triphosphatase , chemistry , adcy9 , adenosine triphosphate , enzyme , biology , microbiology and biotechnology , gene , genome
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.