scholarly journals Super-resolution microscopy reveals arrangement of inner membrane protein complexes in mammalian mitochondria

2021 ◽  
Author(s):  
Catherine S. Palmer ◽  
Jieqiong Lou ◽  
Betty Kouskousis ◽  
Elvis Pandzic ◽  
Alexander J. Anderson ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Complexes ◽  
Super Resolution ◽  
Bimodal Distribution ◽  
Complex Iv ◽  
Inner Membrane ◽  
Mitochondrial Inner Membrane ◽  
Cellular Context ◽  
Inner Membrane Protein ◽  
Super Resolution Microscopy

The mitochondrial inner membrane is a protein rich environment containing large multimeric complexes including complexes of the mitochondrial electron transport chain, mitochondrial translocases and quality control machineries. Although the inner membrane is highly proteinaceous, with 40–60% of all mitochondrial proteins localised to this compartment, little is known about the spatial distribution and organisation of complexes in this environment. We set out to survey the arrangement of inner membrane complexes using stochastic optical reconstruction microscopy (STORM). We show subunits of the TIM23 Complex, Tim23 and Tim44, and the Complex IV subunit COXIV form organised clusters and show distinct properties to the outer membrane protein Tom20. Density based cluster analysis indicated a bimodal distribution of Tim44 that is distinct from Tim23, suggesting distinct TIM23 subcomplexes. COXIV is arranged in larger clusters, that are disrupted upon disruption of Complex IV assembly. Thus, STORM super-resolution microscopy is a powerful approach to examine the nanoscale distribution of mitochondrial inner membrane complexes, providing a “visual” approach to obtaining pivotal information on how mitochondrial complexes exist in a cellular context.

scholarly journals MINSTED fluorescence localization and nanoscopy

2021 ◽  
Author(s):  
Michael Weber ◽  
Marcel Leutenegger ◽  
Stefan Stoldt ◽  
Stefan Jakobs ◽  
Tiberiu S. Mihaila ◽  
...  
Keyword(s):  
Standard Deviation ◽  
Super Resolution ◽  
Diffraction Limit ◽  
Stimulated Emission ◽  
Far Field ◽  
Inner Membrane ◽  
Mitochondrial Inner Membrane ◽  
Molecular Scale ◽  
Localization Precision ◽  
Super Resolution Microscopy

AbstractWe introduce MINSTED, a fluorophore localization and super-resolution microscopy concept based on stimulated emission depletion (STED) that provides spatial precision and resolution down to the molecular scale. In MINSTED, the intensity minimum of the STED doughnut, and hence the point of minimal STED, serves as a movable reference coordinate for fluorophore localization. As the STED rate, the background and the required number of fluorescence detections are low compared with most other STED microscopy and localization methods, MINSTED entails substantially less fluorophore bleaching. In our implementation, 200–1,000 detections per fluorophore provide a localization precision of 1–3 nm in standard deviation, which in conjunction with independent single fluorophore switching translates to a ~100-fold improvement in far-field microscopy resolution over the diffraction limit. The performance of MINSTED nanoscopy is demonstrated by imaging the distribution of Mic60 proteins in the mitochondrial inner membrane of human cells.

scholarly journals Mitochondrial inner membrane protein, Mic60/mitofilin in mammalian organ protection

2018 ◽  
Vol 234 (4) ◽  
pp. 3383-3393 ◽  
Author(s):  
Yansheng Feng ◽  
Ngonidzashe B. Madungwe ◽  
Jean C. Bopassa
Keyword(s):  
Membrane Protein ◽  
Organ Protection ◽  
Inner Membrane ◽  
Mitochondrial Inner Membrane ◽  
Inner Membrane Protein

scholarly journals Identification of the essential yeast protein MIM17, an integral mitochondrial inner membrane protein involved in protein import

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

Reconstitution of the mitochondrial inner membrane protein Cox10 by using inteins

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

scholarly journals SMS1, a high-copy suppressor of the yeast mas6 mutant, encodes an essential inner membrane protein required for mitochondrial protein import.

1994 ◽  
Vol 5 (5) ◽  
pp. 529-538 ◽  
Author(s):  
K R Ryan ◽  
M M Menold ◽  
S Garrett ◽  
R E Jensen
Keyword(s):  
Membrane Protein ◽  
Protein Import ◽  
Mitochondrial Protein ◽  
Mitochondrial Protein Import ◽  
Yeast Saccharomyces Cerevisiae ◽  
Inner Membrane ◽  
Mitochondrial Inner Membrane ◽  
Inner Membrane Protein ◽  
Membrane Spanning ◽  
Membrane Spanning Domains

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.

Gerbils of a seizure-sensitive strain have a mitochondrial inner membrane protein with different isoelectric points from those of a seizure-resistant strain

2002 ◽  
Vol 23 (24) ◽  
pp. 4167-4174 ◽  
Author(s):  
Akira Omori ◽  
Sachiyo Ichinose ◽  
Satoko Kitajima ◽  
Kumiko W. Shimotohno ◽  
Yoshiya L. Murashima ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Resistant Strain ◽  
Sensitive Strain ◽  
Inner Membrane ◽  
Mitochondrial Inner Membrane ◽  
Isoelectric Points ◽  
Inner Membrane Protein
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