scholarly journals Mitochondrial Protection From Ischemia‐Reoxygenation Injury with Mitochondrial Heat Shock Protein 70 Overexpression

2006 ◽  
Vol 20 (5) ◽  
Author(s):  
John Michael Hollander ◽  
Brian T. Scott ◽  
Darrell D. Belke ◽  
Wolfgang H. Dillmann
Polar Biology ◽  
2014 ◽  
Vol 37 (8) ◽  
pp. 1145-1155 ◽  
Author(s):  
Shenghao Liu ◽  
Jing Wang ◽  
Bailin Cong ◽  
Xiaohang Huang ◽  
Kaoshan Chen ◽  
...  

2004 ◽  
Vol 279 (24) ◽  
pp. 25689-25695 ◽  
Author(s):  
Francesca Orsini ◽  
Enrica Migliaccio ◽  
Maurizio Moroni ◽  
Cristina Contursi ◽  
Veronica A. Raker ◽  
...  

1994 ◽  
Vol 127 (4) ◽  
pp. 893-902 ◽  
Author(s):  
J M Herrmann ◽  
R A Stuart ◽  
E A Craig ◽  
W Neupert

Mitochondrial heat shock protein 70 (mt-Hsp70) has been shown to play an important role in facilitating import into, as well as folding and assembly of nuclear-encoded proteins in the mitochondrial matrix. Here, we describe a role for mt-Hsp70 in chaperoning proteins encoded by mitochondrial DNA and synthesized within mitochondria. The availability of mt-Hsp70 function influences the pattern of proteins synthesized in mitochondria of yeast both in vivo and in vitro. In particular, we show that mt-Hsp70 acts in maintaining the var1 protein, the only mitochondrially encoded subunit of mitochondrial ribosomes, in an assembly competent state, especially under heat stress conditions. Furthermore, mt-Hsp70 helps to facilitate assembly of mitochondrially encoded subunits of the ATP synthase complex. By interacting with the ATP-ase 9 oligomer, mt-Hsp70 promotes assembly of ATP-ase 6, and thereby protects the latter protein from proteolytic degradation. Thus mt-Hsp70 by acting as a chaperone for proteins encoded by the mitochondrial DNA, has a critical role in the assembly of supra-molecular complexes.


2000 ◽  
Vol 32 (12) ◽  
pp. 2229-2237 ◽  
Author(s):  
Ken-ichiro Kawana ◽  
Yuki Miyamoto ◽  
Kouichi Tanonaka ◽  
Yoko Han-no ◽  
Hiroyuki Yoshida ◽  
...  

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