叶绿体非典型激酶ABC1K1的功能需要保守的活性位点天冬氨酸残基。
The conserved active site aspartate residue is required for the function of the chloroplast atypical kinase ABC1K1.
作者信息
Turquand Maud, Justo Da Silva Ana Rita, Pralon Thibaut, Longoni Fiamma, Kessler Felix, Collombat Joy
机构信息
Plant Physiology Laboratory, Institute of Biology, Université de Neuchâtel, Neuchâtel, Switzerland.
CDC-LAB, Plan-les-Ouates, Switzerland.
出版信息
Front Plant Sci. 2024 Nov 19;15:1491719. doi: 10.3389/fpls.2024.1491719. eCollection 2024.
INTRODUCTION
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.
METHODS
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.
RESULTS
Complementation of the abc1k1 knock out mutant with ABC1K1 D400N, failed to restore the wildtype phenotype.
DISCUSSION
These results provide in vivo evidence for a critical role of the active site aspartate residue (D400) of ABC1K1.
引言
拟南芥（BC1复合物活性/质子调节6）突变体的特征是由应激性红光以及高光引发的光合和条件性发育表型。拟南芥ABC1样激酶属于非典型激酶家族，包含保守的ATP结合和水解基序，但其生理需求从未被研究过。
方法
通过突变为天冬酰胺，我们证明了ATP结合基序VIIb内高度保守的活性位点天冬氨酸残基是ABC1K1生理功能所必需的。
结果
用ABC1K1 D400N对abc1k1敲除突变体进行互补，未能恢复野生型表型。
讨论
这些结果为ABC1K1活性位点天冬氨酸残基（D400）的关键作用提供了体内证据。
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