scholarly journals The m-AAA Protease Processes Cytochrome c Peroxidase Preferentially at the Inner Boundary Membrane of Mitochondria

2009 ◽  
Vol 20 (2) ◽  
pp. 572-580 ◽  
Author(s):  
Ida E. Suppanz ◽  
Christian A. Wurm ◽  
Dirk Wenzel ◽  
Stefan Jakobs
Keyword(s):  
Cytochrome C ◽  
Protein Quality ◽  
Cytochrome C Peroxidase ◽  
Inner Membrane ◽  
Proteolytic Activation ◽  
Mitochondrial Inner Membrane ◽  
Functional Differences ◽  
Oligomeric Complex ◽  
Quantitative Immunoelectron Microscopy ◽  
Boundary Membrane

The m-AAA protease is a conserved hetero-oligomeric complex in the inner membrane of mitochondria. Recent evidence suggests a compartmentalization of the contiguous mitochondrial inner membrane into an inner boundary membrane (IBM) and a cristae membrane (CM). However, little is known about the functional differences of these subdomains. We have analyzed the localizations of the m-AAA protease and its substrate cytochrome c peroxidase (Ccp1) within yeast mitochondria using live cell fluorescence microscopy and quantitative immunoelectron microscopy. We find that the m-AAA protease is preferentially localized in the IBM. Likewise, the membrane-anchored precursor form of Ccp1 accumulates in the IBM of mitochondria lacking a functional m-AAA protease. Only upon proteolytic cleavage the mature form mCcp1 moves into the cristae space. These findings suggest that protein quality control and proteolytic activation exerted by the m-AAA protease take place preferentially in the IBM pointing to significant functional differences between the IBM and the CM.

scholarly journals Pet191 Is a Cytochrome c Oxidase Assembly Factor in Saccharomyces cerevisiae

2008 ◽  
Vol 7 (8) ◽  
pp. 1427-1431 ◽  
Author(s):  
Oleh Khalimonchuk ◽  
Kevin Rigby ◽  
Megan Bestwick ◽  
Fabien Pierrel ◽  
Paul A. Cobine ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Inner Membrane ◽  
Mitochondrial Inner Membrane ◽  
Disulfide Linkages ◽  
Assembly Factor ◽  
Oligomeric Complex

ABSTRACT The twin-Cx9C motif protein Pet191 is essential for cytochrome c oxidase maturation. The motif Cys residues are functionally important and appear to be present in disulfide linkages within a large oligomeric complex associated with the mitochondrial inner membrane. The import of Pet191 differs from that of other twin-Cx9C motif class of proteins in being independent of the Mia40 pathway.

scholarly journals Mitochondrial Membrane Dynamics—Functional Positioning of OPA1

Antioxidants ◽  
2018 ◽  
Vol 7 (12) ◽  
pp. 186 ◽  
Author(s):  
Hakjoo Lee ◽  
Yisang Yoon
Keyword(s):  
Mitochondrial Membrane ◽  
Proteolytic Cleavage ◽  
Membrane Dynamics ◽  
Mitochondrial Morphology ◽  
Inner Membrane ◽  
Mitochondrial Inner Membrane ◽  
Functional Differences ◽  
New Information ◽  
New Development

The maintenance of mitochondrial energetics requires the proper regulation of mitochondrial morphology, and vice versa. Mitochondrial dynamins control mitochondrial morphology by mediating fission and fusion. One of them, optic atrophy 1 (OPA1), is the mitochondrial inner membrane remodeling protein. OPA1 has a dual role in maintaining mitochondrial morphology and energetics through mediating inner membrane fusion and maintaining the cristae structure. OPA1 is expressed in multiple variant forms through alternative splicing and post-translational proteolytic cleavage, but the functional differences between these variants have not been completely understood. Recent studies generated new information regarding the role of OPA1 cleavage. In this review, we will first provide a brief overview of mitochondrial membrane dynamics by describing fission and fusion that are mediated by mitochondrial dynamins. The second part describes OPA1-mediated fusion and energetic maintenance, the role of OPA1 cleavage, and a new development in OPA1 function, in which we will provide new insight for what OPA1 does and what proteolytic cleavage of OPA1 is for.

scholarly journals Intramitochondrial sorting of the precursor to yeast cytochrome c oxidase subunit Va.

1993 ◽  
Vol 121 (5) ◽  
pp. 1021-1029 ◽  
Author(s):  
B R Miller ◽  
M G Cumsky
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Mitochondrial Protein ◽  
Inner Membrane ◽  
Oxidase Subunit ◽  
Mitochondrial Inner Membrane ◽  
The Matrix ◽  
Inner Membrane Protein ◽  
Membrane Spanning ◽  
Mitochondrial Heat Shock Protein

We have continued our studies on the import pathway of the precursor to yeast cytochrome c oxidase subunit Va (pVa), a mitochondrial inner membrane protein. Previous work on this precursor demonstrated that import of pVa is unusually efficient, and that inner membrane localization is directed by a membrane-spanning domain in the COOH-terminal third of the protein. Here we report the results of studies aimed at analyzing the intramitochondrial sorting of pVa, as well as the role played by ancillary factors in import and localization of the precursor. We found that pVa was efficiently imported and correctly sorted in mitochondria prepared from yeast strains defective in the function of either mitochondrial heat shock protein (hsp)60 or hsp70. Under identical conditions the import and sorting of another mitochondrial protein, the precursor to the beta subunit of the F1 ATPase, was completely defective. Consistent with previous results demonstrating that the subunit Va precursor is loosely folded, we found that pVa could be efficiently imported into mitochondria after translation in wheat germ extracts. This results suggests that normal levels of extramitochondrial hsp70 are also not required for import of the protein. The results of this study enhance our understanding of the mechanism by which pVa is routed to the mitochondrial inner membrane. They suggest that while the NH2 terminus of pVa is exposed to the matrix and processed by the matrix metalloprotease, the protein remains anchored to the inner membrane before being assembled into a functional holoenzyme complex.

scholarly journals The Assembly Pathway of the Mitochondrial Carrier Translocase Involves Four Preprotein Translocases

2008 ◽  
Vol 28 (13) ◽  
pp. 4251-4260 ◽  
Author(s):  
Karina Wagner ◽  
Natalia Gebert ◽  
Bernard Guiard ◽  
Katrin Brandner ◽  
Kaye N. Truscott ◽  
...  
Keyword(s):  
Protein Complexes ◽  
Intermembrane Space ◽  
Inner Membrane ◽  
Mitochondrial Carrier ◽  
Important Principle ◽  
Highly Active ◽  
Mitochondrial Inner Membrane ◽  
Assembly Pathway ◽  
Oligomeric Complex ◽  
The Individual

ABSTRACT The mitochondrial inner membrane contains preprotein translocases that mediate insertion of hydrophobic proteins. Little is known about how the individual components of these inner membrane preprotein translocases combine to form multisubunit complexes. We have analyzed the assembly pathway of the three membrane-integral subunits Tim18, Tim22, and Tim54 of the twin-pore carrier translocase. Tim54 displayed the most complex pathway involving four preprotein translocases. The precursor is translocated across the intermembrane space in a supercomplex of outer and inner membrane translocases. The TIM10 complex, which translocates the precursor of Tim22 through the intermembrane space, functions in a new posttranslocational manner: in case of Tim54, it is required for the integration of Tim54 into the carrier translocase. Tim18, the function of which has been unknown so far, stimulates integration of Tim54 into the carrier translocase. We show that the carrier translocase is built via a modular process and that each subunit follows a different assembly route. Membrane insertion and assembly into the oligomeric complex are uncoupled for each precursor protein. We propose that the mitochondrial assembly machinery has adapted to the needs of each membrane-integral subunit and that the uncoupling of translocation and oligomerization is an important principle to ensure continuous import and assembly of protein complexes in a highly active membrane.

scholarly journals MINOS1 is a conserved component of mitofilin complexes and required for mitochondrial function and cristae organization

2012 ◽  
Vol 23 (2) ◽  
pp. 247-257 ◽  
Author(s):  
Alwaleed K. Alkhaja ◽  
Daniel C. Jans ◽  
Miroslav Nikolov ◽  
Milena Vukotic ◽  
Oleksandr Lytovchenko ◽  
...  
Keyword(s):  
Carbon Sources ◽  
Ultrastructural Level ◽  
Yeast Cells ◽  
Mitochondrial Morphology ◽  
Inner Membrane ◽  
Mitochondrial Inner Membrane ◽  
Inner Membrane Protein ◽  
Protein Rich ◽  
Boundary Membrane ◽  
Insight Into

The inner membrane of mitochondria is especially protein rich and displays a unique morphology characterized by large invaginations, the mitochondrial cristae, and the inner boundary membrane, which is in proximity to the outer membrane. Mitochondrial inner membrane proteins appear to be not evenly distributed in the inner membrane, but instead organize into functionally distinct subcompartments. It is unknown how the organization of the inner membrane is achieved. We identified MINOS1/MIO10 (C1orf151/YCL057C-A), a conserved mitochondrial inner membrane protein. mio10-mutant yeast cells are affected in growth on nonfermentable carbon sources and exhibit altered mitochondrial morphology. At the ultrastructural level, mutant mitochondria display loss of inner membrane organization. Proteomic analyses reveal MINOS1/Mio10 as a novel constituent of Mitofilin/Fcj1 complexes in human and yeast mitochondria. Thus our analyses reveal new insight into the composition of the mitochondrial inner membrane organizing machinery.

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