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Ajala, I.

Publications and source records attributed to Ajala, I..

2 recordsLinked to original sources

Regulation of mitochondrial DNA homeostasis by a mitochondrial microprotein

The actin cytoskeleton and non-muscle myosins coordinate a wide array of cellular functions, yet their contribution to mitochondrial genome maintenance remains poorly understood. Here, we identify AltSLC35A4, a conserved protein encoded by an alternative open reading frame (AltORF), as a novel regulator of mitochondrial DNA (mtDNA) homeostasis. Using co-immunoprecipitation and mass spectrometry, we show that AltSLC35A4 interacts with actomyosin cytoskeletal regulators including MYH9 and MYH10, which have been previously implicated in mtDNA regulation. Loss of AltSLC35A4 increases mtDNA copy number and causes a dispersed spatial distribution of mitochondrial nucleoids, leading to the accumulation of extramitochondrial DNA puncta. Theses alterations occur without detectable changes in TFAM expression and mitochondrial membrane potential, suggesting that the mtDNA dysregulation is independent of mtDNA replication and transcription and mitochondrial bioenergetic state. Our findings uncover a previously unrecognized role for AltSLC35A4 in mitochondrial nucleoids regulation and highlight the functional importance of altORF-encoded proteins in mitochondrial biology.

biochemistry↗

The dual coding gene SLC35A4 protects against oxidative stress

Alternative proteins (AltProts) represent a newly recognized class of biologically active proteins encoded from alternative open reading frames (AltORFs) within already annotated genes. This study focuses on the SLC35A4 gene, which encodes both the reference protein SLC35A4 and the alternative protein AltSLC35A4. Using a combination of microscopy and biochemical analyses, we confirmed the presence of AltSLC35A4 in the inner mitochondrial membrane, resolving previous conflicting reports. Previous studies employing ribosome profiling have revealed that during oxidative stress induced by sodium arsenite, the reference coding sequence of SLC35A4 exhibits the largest increase in translational efficiency among all cellular mRNAs. Our results confirmed this translational upregulation, with the emergence of SLC35A4 protein isoforms during oxidative stress in an upstream ORF-dependent manner. Notably, the expression of AltSLC35A4 remained unchanged during oxidative stress. Knock- out of SLC35A4 enhanced sensitivity to oxidative stress in a rescuable manner, indicating a direct implication for SLC35A4 in stress resistance. In conclusion, our research provides compelling evidence for the functional significance of the dual-coding nature of SLC35A4 for resistance to oxidative stress and highlights the importance of considering AltProts in the functional study of eukaryotic genes.

cell biology↗