Mitochondrial protein import: isolation and characterization of the Saccharomyces cerevisiae MFT1 gene

1991 ◽  
Vol 225 (3) ◽  
pp. 483-491 ◽  
Author(s):  
Jinnie M. Garrett ◽  
Keshav K. Singh ◽  
R. A. Vonder Haar ◽  
Scott D. Emr
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Import ◽  
Mitochondrial Protein ◽  
Mitochondrial Protein Import ◽  
Isolation And Characterization

scholarly journals A Transcriptomic and Proteomic Characterization of the Arabidopsis Mitochondrial Protein Import Apparatus and Its Response to Mitochondrial Dysfunction

2004 ◽  
Vol 134 (2) ◽  
pp. 777-789 ◽  
Author(s):  
Ryan Lister ◽  
Orinda Chew ◽  
May-Nee Lee ◽  
Joshua L. Heazlewood ◽  
Rachel Clifton ◽  
...  
Keyword(s):  
Mitochondrial Dysfunction ◽  
Protein Import ◽  
Mitochondrial Protein ◽  
Mitochondrial Protein Import

scholarly journals Cryo-EM structure of the mitochondrial protein-import channel TOM complex from Saccharomyces cerevisiae

2019 ◽  
Author(s):  
Kyle Tucker ◽  
Eunyong Park
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Import ◽  
Protein Translocation ◽  
Mitochondrial Protein ◽  
Nuclear Genome ◽  
Molecular Organization ◽  
Mitochondrial Outer Membrane ◽  
Mitochondrial Protein Import ◽  
Tom Complex ◽  
Polar Interactions

AbstractNearly all mitochondrial proteins are encoded by the nuclear genome and imported into mitochondria following synthesis on cytosolic ribosomes. These precursor proteins are translocated into mitochondria by the TOM complex, a protein-conducting channel in the mitochondrial outer membrane. Using cryo-EM, we have obtained high-resolution structures of both apo and presequence-bound core TOM complexes from Saccharomyces cerevisiae in dimeric and tetrameric forms. Dimeric TOM consists of two copies each of five proteins arranged in two-fold symmetry—Tom40, a pore-forming β-barrel with an overall negatively-charged inner surface, and four auxiliary α-helical transmembrane proteins. The structure suggests that presequences for mitochondrial targeting insert into the Tom40 channel mainly by electrostatic and polar interactions. The tetrameric complex is essentially a dimer of dimeric TOM, which may be capable of forming higher-order oligomers. Our study reveals the molecular organization of the TOM complex and provides new insights about the mechanism of protein translocation into mitochondria.

Characterization of the Novel Mitochondrial Protein Import Component, Tom34, in Mammalian Cells

1999 ◽  
Vol 125 (4) ◽  
pp. 721-727 ◽  
Author(s):  
N. Chewawiwat ◽  
M. Yano ◽  
K. Terada ◽  
N. J Hoogenraad ◽  
M. Mori
Keyword(s):  
Mammalian Cells ◽  
Protein Import ◽  
Mitochondrial Protein ◽  
The Novel ◽  
Mitochondrial Protein Import
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