Amberg_2025_rawdata
<p dir="ltr"><u>Background:</u> Mitochondria carry out essential functions in eukaryotic cells. The mitochondrial genome encodes factors critical to support oxidative phosphorylation and mitochondrial protein import necessary for these functions. However, organisms like b...
محفوظ في:
| المؤلف الرئيسي: | |
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| منشور في: |
2025
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| الموضوعات: | |
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إضافة وسم
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| الملخص: | <p dir="ltr"><u>Background:</u> Mitochondria carry out essential functions in eukaryotic cells. The mitochondrial genome encodes factors critical to support oxidative phosphorylation and mitochondrial protein import necessary for these functions. However, organisms like budding yeast can readily lose their mitochondrial genome, yielding respiration-deficient <i>petite</i> mutants. The fission yeast <i>Schizosaccharomyces pombe</i> is <i>petite</i>-negative, but some nuclear mutations enable the loss of its mitochondrial genome.</p><p dir="ltr"><u>Results:</u> Here, we characterize the classical <i>petite</i>-positive mutation <i>ptp1-1</i> as a loss of function allele of the proteasome 19S regulatory subunit component <i>mts4/rpn1</i>, involved in the ubiquitin-dependent degradation pathway. By comparison with another petite-enabling mutation in the g-subunit of the F<sub>1</sub>-ATPase, we show that <i>ptp1-1</i> does not rescue mitochondrial membrane potential. Instead, the mutation results in increased levels of mitochondrial and cytoplasmic chaperones and an altered oxidative stress response.</p><p dir="ltr"><u>Conclusions:</u> <i>ptp1-1</i> is a partial loss of function mutation of the proteasome that enables growth of cells devoid of mitochondrial DNA through a mechanism that is independent of mitochondrial membrane potential rescue and associated with proteasome dependent regulation of mitochondrial protein import precursors and the oxidative stress response.</p> |
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