AI Article Synopsis

  • Numerous studies indicate that stress impacts plant cell components, particularly RNA editing associated with electron transport chains.
  • The mitochondrial ATP synthase complex, crucial for cellular respiration, includes a b subunit encoded by a specific mitochondrial gene, which was analyzed for RNA editing effects under various conditions.
  • Findings revealed that RNA editing influenced the b subunit's structure, enhancing hydrogen ion selectivity and potentially stabilizing the complex, suggesting the edits aim to restore functionality rather than simply responding to salt stress.

Article Abstract

Numerous studies have shown that stress in plant cells and organelles with transport electron chains is related to RNA editing. The ATP synthase complex present in mitochondria plays a crucial role in cellular respiration and consists of several subunits. Among them is the b subunit, which is encoded by the mitochondrial gene. Computing-based analysis of the effects of RNA editing of the gene in mitochondria leading to alterations in the b subunit of ATP synthase. Using the CLC Genomic Workbench 3, RNA editing analysis between the control and salt stress conditions was not significantly different. Depending on RNA editing, the tertiary structure model revealed a change in the states of the b subunit, reflecting differences in the central stalk and F1-catalytic domain. The study found that polar edits in the N-terminus of the b subunit allow for efficient H + ion selectivity and introduce a new coiled-coil alpha-helical structure that may help stabilize the complex. The most noteworthy finding of this study was the strong impact of these editing events on the tertiary structure of the b subunit, which has the potential to affect the ATPase activity and indicate that the editing in this subunit aimed to restore the original active protein and not as a response to salt stress.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10570708PMC
http://dx.doi.org/10.1016/j.sjbs.2023.103817DOI Listing

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