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

The Arabidopsis (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...

Full description

Saved in:
Bibliographic Details
Published in:Frontiers in plant science 2024-11, Vol.15, p.1491719
Main Authors: Turquand, Maud, Justo Da Silva, Ana Rita, Pralon, Thibaut, Longoni, Fiamma, Kessler, Felix, Collombat, Joy
Format: Article
Language:English
Subjects:
active site mutation
atypical kinase ABC1K1
chloroplast
complementation
photosynthesis
Plant Science
Citations: Items that this one cites
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The Arabidopsis (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. 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. Complementation of the abc1k1 knock out mutant with ABC1K1 D400N, failed to restore the wildtype phenotype. These results provide in vivo evidence for a critical role of the active site aspartate residue (D400) of ABC1K1.
ISSN:1664-462X
1664-462X
DOI:10.3389/fpls.2024.1491719