Protein translocation in mitochondria: Sorting out the Toms, Tims, Pams, Sams and Mia

Herrmann, J. M.; Bykov, Yury S.

doi:10.1002/1873-3468.14614

Cited by 15 publications

(2 citation statements)

References 28 publications

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“…Mitochondrial porins are similar to most mitochondrial proteins encoded by the nucleus, synthesized at cytoplasmic ribosomes, and transported post-translationally into mitochondria [ 65 , 66 ]. The heterologous expression of eukaryotic porins in E. coli offers an elegant method for the mass production of mitochondrial porins that are needed for structural studies and electrophysiology.…”

Section: Heterologous Expression Of Mitochondrial Porins In ...mentioning

confidence: 99%

Solute Transport through Mitochondrial Porins In Vitro and In Vivo

Benz

2024

Biomolecules

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Mitochondria are most likely descendants of strictly aerobic prokaryotes from the class Alphaproteobacteria. The mitochondrial matrix is surrounded by two membranes according to its relationship with Gram-negative bacteria. Similar to the bacterial outer membrane, the mitochondrial outer membrane acts as a molecular sieve because it also contains diffusion pores. However, it is more actively involved in mitochondrial metabolism because it plays a functional role, whereas the bacterial outer membrane has only passive sieving properties. Mitochondrial porins, also known as eukaryotic porins or voltage-dependent anion-selective channels (VDACs) control the permeability properties of the mitochondrial outer membrane. They contrast with most bacterial porins because they are voltage-dependent. They switch at relatively small transmembrane potentials of 20 to 30 mV in closed states that exhibit different permeability properties than the open state. Whereas the open state is preferentially permeable to anionic metabolites of mitochondrial metabolism, the closed states prefer cationic solutes, in particular, calcium ions. Mitochondrial porins are encoded in the nucleus, synthesized at cytoplasmatic ribosomes, and post-translationally imported through special transport systems into mitochondria. Nineteen beta strands form the beta-barrel cylinders of mitochondrial and related porins. The pores contain in addition an α-helical structure at the N-terminal end of the protein that serves as a gate for the voltage-dependence. Similarly, they bind peripheral proteins that are involved in mitochondrial function and compartment formation. This means that mitochondrial porins are localized in a strategic position to control mitochondrial metabolism. The special features of the role of mitochondrial porins in apoptosis and cancer will also be discussed in this article.

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Section: Heterologous Expression Of Mitochondrial Porins In ...mentioning

confidence: 99%

Solute Transport through Mitochondrial Porins In Vitro and In Vivo

Benz

2024

Biomolecules

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“…In addition, mitochondrial proteins are distributed to different sub-locations inside the organelle: outer membrane (OM), intermembrane space (IMS), inner membrane (IM), and matrix. Most of the proteins are produced in the cytosol and are imported based on the targeting signals encoded in their amino acid sequence (Herrmann & Bykov, 2023). On the OM these signals are recognized and threaded through by the translocase of the outer membrane (TOM) complex.…”

Section: Introductionmentioning

confidence: 99%

A systematic bi-genomic split-GFP assay illuminates the mitochondrial matrix proteome and protein targeting routes

Bykov,

Zuttion,

Senger

et al. 2024

Preprint

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The majority of mitochondrial proteins are encoded in the nuclear genome and often lack clear targeting signals. Therefore, what constitutes the entire mitochondrial proteome is still unclear. We here build on our previously developed bi-genomic (BiG) split-GFP assay (Bader et al. 2020) to solidify the list of matrix and inner membrane mitochondrial proteins. The assay relies on one fragment (GFP1-10) encoded in the mitochondrial DNA enabling specific visualization of only the proteins tagged with a smaller fragment, GFP11, and localized to the mitochondrial matrix or the inner membrane. We used the SWAp-Tag (SWAT) strategy to tag every protein with GFP11 and mated them with the BiG GFP strain. Imaging the collection in six different conditions allowed us to visualize almost 400 mitochondrial proteins, 50 of which were never visualized in mitochondria before, and many are poorly studied dually localized proteins. We also show how this data can be applied to study mitochondrial inner membrane protein topology and sorting. This work brings us closer to finalizing the mitochondrial proteome and the freely distributed library of GFP11-tagged strains will be a useful resource to study protein localization, biogenesis and interactions.

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Translocation of Proteins into Four Membrane-Bound Complex Plastids of Red Algal Origin

Gruber,

Kroth

2024

Endosymbiotic Organelle Acquisition

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Protein translocation in mitochondria: Sorting out the Toms, Tims, Pams, Sams and Mia

Cited by 15 publications

References 28 publications

Solute Transport through Mitochondrial Porins In Vitro and In Vivo

Solute Transport through Mitochondrial Porins In Vitro and In Vivo

A systematic bi-genomic split-GFP assay illuminates the mitochondrial matrix proteome and protein targeting routes

Translocation of Proteins into Four Membrane-Bound Complex Plastids of Red Algal Origin

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