Blue Native electrophoresis to study mitochondrial and other protein complexes

Methods ◽  
2002 ◽  
Vol 26 (4) ◽  
pp. 327-334 ◽  
Author(s):  
L Nijtmans
2013 ◽  
Vol 60 (4) ◽  
pp. 563-570
Author(s):  
T. A. Shevyreva ◽  
M. S. Piotrovskii ◽  
B. V. Belugin ◽  
I. M. Zhestkova ◽  
M. S. Trofimova

Author(s):  
Juliana Heidler ◽  
Valentina Strecker ◽  
Florian Csintalan ◽  
Lea Bleier ◽  
Ilka Wittig

2005 ◽  
Vol 40 (9) ◽  
pp. 1223-1231 ◽  
Author(s):  
Anabel S. Fandiño ◽  
Isam Rais ◽  
Martin Vollmer ◽  
Helmuth Elgass ◽  
Hermann Schägger ◽  
...  

2000 ◽  
Vol 11 (1) ◽  
pp. 103-116 ◽  
Author(s):  
Oliver Kerscher ◽  
Naresh B. Sepuri ◽  
Robert E. Jensen

The mitochondrial inner membrane contains two separate translocons: one required for the translocation of matrix-targeted proteins (the Tim23p-Tim17p complex) and one for the insertion of polytopic proteins into the mitochondrial inner membrane (the Tim54p-Tim22p complex). To identify new members of the Tim54p-Tim22p complex, we screened for high-copy suppressors of the temperature-sensitivetim54-1 mutant. We identified a new gene,TIM18, that encodes an integral protein of the inner membrane. The following genetic and biochemical observations suggest that the Tim18 protein is part of the Tim54p-Tim22p complex in the inner membrane: multiple copies of TIM18 suppress thetim54-1 growth defect; thetim18::HIS3 disruption is synthetically lethal with tim54-1; Tim54p and Tim22p can be coimmune precipitated with the Tim18 protein; and Tim18p, along with Tim54p and Tim22p, is detected in an ∼300-kDa complex after blue native electrophoresis. We propose that Tim18p is a new component of the Tim54p-Tim22p machinery that facilitates insertion of polytopic proteins into the mitochondrial inner membrane.


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