AUTHOR=Turquand Maud , Justo Da Silva Ana Rita , Pralon Thibaut , Longoni Fiamma , Kessler Felix , Collombat Joy 

TITLE=The conserved active site aspartate residue is required for the function of the chloroplast atypical kinase ABC1K1

JOURNAL=Frontiers in Plant Science

VOLUME=15

YEAR=2024

URL=https://www.frontiersin.org/journals/plant-science/articles/10.3389/fpls.2024.1491719

DOI=10.3389/fpls.2024.1491719

ISSN=1664-462X

ABSTRACT=<sec><title>Introduction</title><p>The Arabidopsis <italic>abc1k1/pgr6</italic> (Activity of BC1 complex/proton regulation 6) mutant is characterized by photosynthetic and conditional developmental phenotypes triggered by stressful red as well as high light. The Arabidopsis ABC1-like kinases belong to the atypical kinase family and contain conserved ATP-binding and hydrolysis motifs, but their physiological requirement has never been investigated.</p></sec><sec><title>Methods</title><p>By mutation to asparagine, we demonstrate that the highly conserved active site aspartate residue within ATP-binding motif VIIb is required for the physiological functions of ABC1K1.</p></sec><sec><title>Results</title><p>Complementation of the abc1k1 knock out mutant with ABC1K1 D400N, failed to restore the wildtype phenotype.</p></sec><sec><title>Discussion</title><p>These results provide in vivo evidence for a critical role of the active site aspartate residue (D400) of ABC1K1.</p></sec>