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The constraints of allotopic expression.

Felipe Nieto-Panqueva1, Diana Rubalcava-Gracia2, Patrice P Hamel3

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Summary

Allotopic expression, the transfer of organellar genes to the nucleus, requires careful consideration of protein insertion and topology. This study reviews constraints for mitochondrial gene expression, focusing on OXPHOS subunits and the TIM23 translocator.

Keywords:
Allotopic expressionApparent free energy of membrane insertionMembrane embedded proteinsMitochondrial complexesOxidative phosphorylationProtein importTIM23Transmembrane stretches

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Area of Science:

  • Mitochondrial biology
  • Molecular genetics
  • Protein biophysics

Background:

  • Allotopic expression involves nuclear transfer of organellar genes, followed by cytosolic synthesis and organellar import.
  • Mitochondrial genes encoding OXPHOS subunits are a key focus for studying allotopic expression.
  • Previous studies on allotopic expression may have overlooked critical biophysical and mechanistic constraints.

Purpose of the Study:

  • To critically review experimental evidence for allotopic expression of mitochondrial OXPHOS genes.
  • To highlight overlooked constraints in modifying mitochondrial genes for nuclear expression.
  • To propose design principles for successful allotopic expression of mitochondrial proteins.

Main Methods:

  • Review of experimental data on allotopic expression of OXPHOS subunits.
  • Analysis of codon usage, mitochondrial targeting signals, and protein topology.
  • Application of the biological hydrophobicity scale to predict membrane insertion energy (μΔGapp) of transmembrane stretches (TMS).
  • Evaluation of the role of the TIM23 translocator in protein sorting and topology determination.

Main Results:

  • Successful allotopic expression requires adaptation of codon usage and inclusion of targeting signals.
  • The average apparent free energy of membrane insertion (μΔGapp) of TMS and final protein topology are critical.
  • The TIM23 translocator imposes mechanistic constraints, dictating protein sorting pathways and final topology.
  • A 'traffic light' color code based on μΔGapp predicts mitochondrial import likelihood for allotopically expressed OXPHOS proteins.

Conclusions:

  • Designing proteins for allotopic expression must account for TMS hydrophobicity (μΔGapp) and functional topology.
  • The TIM23 sorting mechanism significantly influences the success of allotopic expression.
  • Maximizing μΔGapp for hydrophobic TMS is crucial for proteins whose genes have not been transferred to the nucleus.
  • This work provides a framework for predicting and engineering successful allotopic expression of mitochondrial proteins.