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Porin Insertion in the Outer Mitochondrial Membrane01:12

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Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
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The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria.  In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...
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Among all the organelles in an animal cell, only mitochondria have their own independent genomes. Animal mitochondrial DNA is a double-stranded, closed-circular molecule with around 20,000 base pairs. Mitochondrial DNA is unique in that one of its two strands, the heavy, or H, -strand is guanine rich, whereas the complementary strand is cytosine rich and called the light, or L, -strand. Compared to nuclear DNA, mitochondrial DNA has a very low percentage of non-coding regions and is marked by...
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A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...
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Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
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Author Spotlight: Oxygen-Independent Assays to Measure Mitochondrial Function in Mammals
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Independent evolution of functionally exchangeable mitochondrial outer membrane import complexes.

Daniela G Vitali1, Sandro Käser2, Antonia Kolb1

  • 1Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.

Elife
|June 21, 2018
PubMed
Summary
This summary is machine-generated.

The fungi-specific Mim1/Mim2 complex and trypanosome pATOM36 protein are functional analogs for mitochondrial outer membrane protein insertion. These proteins evolved convergently in distinct eukaryotic lineages.

Keywords:
MIM complexS. cerevisiaebiochemistrybiogenesischemical biologymitochondriaouter membranetrypanosome

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Evolutionary Biology

Background:

  • Mitochondrial outer membrane (MOM) protein assembly is crucial for organelle function.
  • The fungi-specific Mim1/Mim2 complex mediates the insertion of key MOM proteins.
  • The functional equivalents of Mim1/Mim2 in other eukaryotes remained unknown.

Purpose of the Study:

  • To identify and characterize the functional analogue of the Mim1/Mim2 complex in trypanosomes.
  • To investigate the evolutionary origins of MOM protein insertion machinery.

Main Methods:

  • Reciprocal genetic complementation experiments between yeast and trypanosomes.
  • Analysis of protein complex formation via heterologous expression.
  • Assessment of mitochondrial biogenesis, morphology, and protein assembly defects.

Main Results:

  • Trypanosome MOM protein pATOM36 functionally complements yeast Mim1/Mim2 deletion mutants.
  • Yeast Mim1/Mim2 complex rescues MOM protein assembly defects in pATOM36-deficient trypanosomes.
  • pATOM36 and Mim1/Mim2 form stable complexes independently of other proteins.

Conclusions:

  • pATOM36 is the functional analogue of the yeast Mim1/Mim2 complex in trypanosomes.
  • These proteins represent a case of convergent evolution, arising independently after the divergence of fungi and trypanosomatids.