scholarly journals Plant Mitochondrial Inner Membrane Protein Insertion

2018 ◽  
Vol 19 (2) ◽  
pp. 641 ◽  
Author(s):  
Renuka Kolli ◽  
Jürgen Soll ◽  
Chris Carrie
2000 ◽  
Vol 28 (4) ◽  
pp. 495-499 ◽  
Author(s):  
K. Tokatlidis ◽  
S. Vial ◽  
P. Luciano ◽  
M. Vergnolle ◽  
S. Clémence

The protein import pathway that targets proteins to the mitochondrial matrix has been extensively characterized in the past 15 years. Variations of this import pathway account for the sorting of proteins to other compartments as well, but the insertion of integral inner membrane proteins lacking a presequence is mediated by distinct translocation machinery. This consists of a complex of Tim9 and Tim10, two homologous, Zn2+-binding proteins that chaperone the passage of the hydrophobic precursor across the aqueous inter-membrane space. The precursor is then targeted to another, inner-membrane-bound, complex of at least five subunits that facilitates insertion. Biochemical and genetic experiments have identified the key components of this process; we are now starting to understand the molecular mechanism. This review highlights recent advances in this new membrane protein insertion pathway.


2018 ◽  
Vol 234 (4) ◽  
pp. 3383-3393 ◽  
Author(s):  
Yansheng Feng ◽  
Ngonidzashe B. Madungwe ◽  
Jean C. Bopassa

FEBS Letters ◽  
1994 ◽  
Vol 349 (2) ◽  
pp. 215-221 ◽  
Author(s):  
Ammy C. Maarse ◽  
Jolanda Blom ◽  
Petra Keil ◽  
Nikolaus Pfanner ◽  
Michiel Meijer

Mitochondrion ◽  
2011 ◽  
Vol 11 (4) ◽  
pp. 677
Author(s):  
R. Marco-Lázaro⁎ ◽  
A. Pérez-Martos ◽  
P. Fernández-Silva ◽  
J.A. Enriquez

1994 ◽  
Vol 5 (5) ◽  
pp. 529-538 ◽  
Author(s):  
K R Ryan ◽  
M M Menold ◽  
S Garrett ◽  
R E Jensen

MAS6 encodes an essential inner membrane protein required for mitochondrial protein import in the yeast Saccharomyces cerevisiae (Emtage and Jensen, 1993). To identify new inner membrane import components, we isolated a high-copy suppressor (SMS1) of the mas6-1 mutant. SMS1 encodes a 16.5-kDa protein that contains several potential membrane-spanning domains. The Sms1 protein is homologous to the carboxyl-terminal domain of the Mas6 protein. Like Mas6p, Sms1p is located in the mitochondrial inner membrane and is an essential protein. Depletion of Sms1p from cells causes defects in the import of several mitochondrial precursor proteins, suggesting that Sms1p is a new inner membrane import component. Our observations raise the possibility that Sms1p and Mas6p act together to translocate proteins across the inner membrane.


2002 ◽  
Vol 23 (24) ◽  
pp. 4167-4174 ◽  
Author(s):  
Akira Omori ◽  
Sachiyo Ichinose ◽  
Satoko Kitajima ◽  
Kumiko W. Shimotohno ◽  
Yoshiya L. Murashima ◽  
...  

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