Journal ArticleDOI
Protein translocation into mitochondria.
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TLDR
The biogenesis of mitochondria requires the translocation of most mitochondrial proteins across two biological membranes through three large integral membrane protein complexes forming specialized preprotein translocases.Abstract:
The biogenesis of mitochondria requires the translocation of most mitochondrial proteins across two biological membranes. Mitochondrial preproteins are synthesized in the cytosol carrying targeting inread more
Citations
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Estrogenic control of mitochondrial function and biogenesis
TL;DR: The nuclear effects of estrogens on gene expression directly controlling mitochondrial biogenesis, oxygen consumption, mtDNA transcription, and apoptosis are reviewed.
Journal ArticleDOI
Bacterial endotoxin lipopolysaccharide and reactive oxygen species inhibit leydig cell steroidogenesis via perturbation of mitochondria
TL;DR: The acute effects of LPS demonstrate how sensitive Leydig cell mitochondrial steroidogenesis is to inflammation-induced oxidative stress and the necessity of having respiring mitochondria with an intact Δψm to facilitate StAR function and Leydigs cell steroidogenesis.
Journal ArticleDOI
Estrogens regulate life and death in mitochondria
TL;DR: The mechanisms of rapid and longer-term effects of estrogens and selective ER modulators (SERMs, e.g., tamoxifen (TAM)) on mitochondrial biogenesis, morphology, and function including regulation of Nuclear Respiratory Factor-1 (NRF-1, NRF1) transcription are reviewed.
Journal ArticleDOI
Presenilin-1 is located in rat mitochondria
Maria Ankarcrona,Kjell Hultenby +1 more
TL;DR: It is reported that presenilins PS1 is also located in mitochondrial membranes, and PS1 mutations may make cells more vulnerable to apoptotic stimuli due to dysfunction of this protein at the mitochondrial level.
Journal ArticleDOI
Two domains are critical for the nuclear localization of soluble adenylyl cyclase
TL;DR: The findings provide evidence that these two domains are critical for the nuclear localization of sAC and they collocated with the catalytic domains.
References
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Journal ArticleDOI
Molecular chaperones in cellular protein folding.
TL;DR: Significant progress has been made in the understanding of the ATP-dependent mechanisms used by the Hsp70 and chaperonin families of molecular chaperones, which can cooperate to assist in folding new polypeptide chains.
Journal ArticleDOI
Protein import into mitochondria.
TL;DR: Molecular chaperones in the matrix exert multiple functions in translocation, sorting, folding, and assembly of newly imported proteins.
Journal ArticleDOI
HSP100/Clp proteins: a common mechanism explains diverse functions
TL;DR: The HSP100/Clp proteins are a newly discovered family with a great diversity of functions, such as increased tolerance to high temperatures, promotion of proteolysis of specific cellular substrates and regulation of transcription.
Journal ArticleDOI
Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20.
Yoshito Abe,Toshihiro Shodai,Takanori Muto,Katsuyoshi Mihara,Hisayoshi Torii,Shuh Ichi Nishikawa,Toshiya Endo,Daisuke Kohda +7 more
TL;DR: In this article, the NMR structure of a general import receptor, rat Tom20, in a complex with a presequence peptide derived from rat aldehyde dehydrogenase was reported.
Journal ArticleDOI
Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins
Kerstin Hill,Kirstin Model,Michael T. Ryan,Klaus Dietmeier,Falk Martin,Richard Wagner,Nikolaus Pfanner +6 more
TL;DR: It is concluded that Tom40 is the pore-forming subunit of the mitochondrial general import pore and that it constitutes a hydrophilic, ∼22 Å wide channel for the import of preproteins.
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