Proteinimport über die mitochondriale Innenmembran

Abstract The majority of mitochondrial proteins are nuclear-encoded and translated in the cytosol with an amino-terminal targeting signal called a presequence. Mitochondrial presequences are able to form amphiphilic α-helices with a positively charged and a hydrophobic side. The essential presequence translocase subunit Tim17 forms a cavity exposed to the bilayer, which harbors a negatively charged patch to initiate the translocation of positively charged presequences across the inner membrane.

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Publication Details

Journal
BIOspektrum
Published
2024-09-01
DOI
https://doi.org/10.1007/s12268-024-2256-0
Primary Topic
Mitochondrial Function and Pathology
Type
article
Field-Weighted Citation Impact
0.00
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article

Proteinimport über die mitochondriale Innenmembran

Jakob D. Busch, Laura F. Fielden, Nils Wiedemann, Martin van der Laan
BIOspektrum
Mitochondrial Function and Pathology
article

Proteinimport über die mitochondriale Innenmembran

Jakob D. Busch, Laura F. Fielden, Nils Wiedemann, Martin van der Laan
article en

Abstract

Abstract The majority of mitochondrial proteins are nuclear-encoded and translated in the cytosol with an amino-terminal targeting signal called a presequence. Mitochondrial presequences are able to form amphiphilic α-helices with a positively charged and a hydrophobic side. The essential presequence translocase subunit Tim17 forms a cavity exposed to the bilayer, which harbors a negatively charged patch to initiate the translocation of positively charged presequences across the inner membrane.

BIOspektrumVol. 30(5)
University of Freiburg (DE), Saarland University (DE)
Openalex Percentile: Top 86%
Mitochondrial Function and Pathology
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