scholarly journals ATAD3A has a scaffolding role regulating mitochondria inner membrane structure and protein assembly

Cell Reports ◽  
2021 ◽  
Vol 37 (12) ◽  
pp. 110139
Author(s):  
Tania Arguello ◽  
Susana Peralta ◽  
Hana Antonicka ◽  
Gabriel Gaidosh ◽  
Francisca Diaz ◽  
...  
Keyword(s):  
Membrane Structure ◽  
Protein Assembly ◽  
Inner Membrane

scholarly journals A novel algorithm identifies stress-induced alterations in mitochondrial connectivity and inner membrane structure from confocal images

2017 ◽  
Vol 13 (6) ◽  
pp. e1005612 ◽  
Author(s):  
Mathieu Ouellet ◽  
Gérald Guillebaud ◽  
Valerie Gervais ◽  
David Lupien St-Pierre ◽  
Marc Germain
Keyword(s):  
Membrane Structure ◽  
Inner Membrane ◽  
Confocal Images ◽  
Novel Algorithm

scholarly journals ROMO1 is a constituent of the human presequence translocase required for YME1L protease import

2018 ◽  
Vol 218 (2) ◽  
pp. 598-614 ◽  
Author(s):  
Frank Richter ◽  
Sven Dennerlein ◽  
Miroslav Nikolov ◽  
Daniel C. Jans ◽  
Nataliia Naumenko ◽  
...  
Keyword(s):  
Membrane Structure ◽  
Protein Import ◽  
Protein Quality ◽  
Functional Characterization ◽  
Mitochondrial Protein ◽  
Mitochondrial Protein Import ◽  
Yeast Saccharomyces Cerevisiae ◽  
Inner Membrane ◽  
Inner Membrane Protein ◽  
General Protein

The mitochondrial presequence translocation machinery (TIM23 complex) is conserved between the yeast Saccharomyces cerevisiae and humans; however, functional characterization has been mainly performed in yeast. Here, we define the constituents of the human TIM23 complex using mass spectrometry and identified ROMO1 as a new translocase constituent with an exceptionally short half-life. Analyses of a ROMO1 knockout cell line revealed aberrant inner membrane structure and altered processing of the GTPase OPA1. We show that in the absence of ROMO1, mitochondria lose the inner membrane YME1L protease, which participates in OPA1 processing and ROMO1 turnover. While ROMO1 is dispensable for general protein import along the presequence pathway, we show that it participates in the dynamics of TIM21 during respiratory chain biogenesis and is specifically required for import of YME1L. This selective import defect can be linked to charge distribution in the unusually long targeting sequence of YME1L. Our analyses establish an unexpected link between mitochondrial protein import and inner membrane protein quality control.

Cytochrome Function in Relation to Inner Membrane Structure of Mitochondria

Science ◽  
1963 ◽  
Vol 142 (3596) ◽  
pp. 1176-1179 ◽  
Author(s):  
B. Chance ◽  
D. F. Parsons
Keyword(s):  
Membrane Structure ◽  
Inner Membrane

scholarly journals PtdIns 3-Kinase Orchestrates Autophagosome Formation in Yeast

2011 ◽  
Vol 2011 ◽  
pp. 1-9 ◽  
Author(s):  
Keisuke Obara ◽  
Yoshinori Ohsumi
Keyword(s):  
Membrane Structure ◽  
Protein Complexes ◽  
Eukaryotic Cells ◽  
Autophagosome Formation ◽  
Inner Membrane ◽  
Double Membrane ◽  
Atg Proteins ◽  
Related Proteins ◽  
Lytic Compartment ◽  
Enzymatic Product

Eukaryotic cells can massively transport their own cytoplasmic contents into a lytic compartment, the vacuole/lysosome, for recycling through a conserved system called autophagy. The key process in autophagy is the sequestration of cytoplasmic contents within a double-membrane structure, the autophagosome. Autophagosome formation requires the elaborate cooperation of Atg (autophagy-related) proteins and lipid molecules. Phosphorylation of phosphatidylinositol (PtdIns) by a PtdIns 3-kinase, Vps34, is a key step in coordinating Atg proteins and lipid molecules. Vps34 forms two distinct protein complexes, only one of which is involved in generating autophagic membranes. Upon induction of autophagy, PtdIns(3)P, the enzymatic product of PtdIns 3-kinase, is massively transported into the lumen of the vacuoleviaautophagy. PtdIns(3)Pis enriched on the inner membrane of the autophagosome. PtdIns(3)Precruits the Atg18−Atg2 complex and presumably other Atg proteins to autophagic membranes, thereby coordinating lipid molecules and Atg proteins.

scholarly journals A novel capsid protein network allows the characteristic inner membrane structure of Marseilleviridae giant viruses

2021 ◽  
Author(s):  
Akane Chihara ◽  
Raymond N. Burton-Smith ◽  
Naoko Kajimura ◽  
Kaoru Mitsuoka ◽  
Kenta Okamoto ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Membrane Structure ◽  
Scaffold Proteins ◽  
Protein Network ◽  
Particle Analysis ◽  
New Order ◽  
Inner Membrane ◽  
Novel Structure ◽  
Giant Viruses ◽  
Icosahedral Particle

AbstractMarseilleviridae is a family of the new order of giant viruses, which exhibit a characteristic inner membrane. Here, we investigated the entire structure of tokyovirus, a species of Marseillevirus at 7.7 Å resolution using 1 MV high-voltage cryo-EM and single particle analysis. The minor capsid lattice formed by five proteins, shows a novel structure compared to other icosahedral giant viruses. Under the minor capsid proteins, scaffold proteins connect two five-fold vertices and interact with the inner membrane. Previously reported giant viruses utilise “tape measure” proteins, proposed to control its capsid size, which could not be identified in tokyovirus, but scaffold proteins appear to perform a similar role. A density on top of the major capsid protein was identified, which suggested to be a 14kDa glycoprotein. Our observations suggest that the icosahedral particle of Marseilleviridae is constructed with a novel capsid protein network, which allows the characteristic inner membrane structure.

Design and optimisation of the external load bearing carry through structure of a columned multi bubble fuselage

2013 ◽  
Vol 117 (1187) ◽  
pp. 97-108
Author(s):  
S. H. Cho ◽  
C. Bil ◽  
R. Adams
Keyword(s):  
Finite Element ◽  
Structural Design ◽  
Membrane Structure ◽  
Finite Element Models ◽  
Design Domain ◽  
Inner Membrane ◽  
And Topology ◽  
Bending Loads ◽  
Design Challenge ◽  
The Given

Abstract The blended wing-body configuration holds a major structural design challenge at the centre-body where the structure must support both wing bending loads and internal cabin pressure. A membrane approach is proposed which decouples the loads to allow their resistance by two independent structures: an inner membrane for cabin pressure and an outer structure to resist wing loads. A columned multi-bubble fuselage is proposed for the inner membrane structure, which are multispherical configuration to efficiently withstand the pressure loads. Considering this configuration, the carry-through structure can be designed and optimised. Finite element results show a significant reduction of stress level in this design over that for a conventional multi-bubble fuselage. Up to 30% weight reduction is achieved for a military cargo application that requires an extensive area with no structural interruption. For the outer carry-through structure, the topology and shape optimisations of finite element models were performed on the given design domain. The results from the shape and topology optimisations were complementary demonstrating a consistent design approach. The optimisation theory is briefly presented along with the results.

Development and function of plasmodesmata in zygotes of Fucus distichus

2015 ◽  
Vol 58 (3) ◽  
Author(s):  
Chikako Nagasato ◽  
Makoto Terauchi ◽  
Atsuko Tanaka ◽  
Taizo Motomura
Keyword(s):  
Endoplasmic Reticulum ◽  
Simple Form ◽  
Brown Algae ◽  
Membrane Structure ◽  
Inner Membrane ◽  
Green Plants ◽  
Fucus Distichus ◽  
And Function ◽  
20 Nm

AbstractBrown algae have plasmodesmata, tiny tubular cytoplasmic channels connecting adjacent cells. The lumen of plasmodesmata is 10–20 nm wide, and it takes a simple form, without a desmotubule (the inner membrane structure consisting of endoplasmic reticulum in the plasmodesmata of green plants). In this study, we analyzed the ultrastructure and distribution of plasmodesmata during development of

scholarly journals Loss of OPA1 Perturbates the Mitochondrial Inner Membrane Structure and Integrity, Leading to CytochromecRelease and Apoptosis

2002 ◽  
Vol 278 (10) ◽  
pp. 7743-7746 ◽  
Author(s):  
Aurélien Olichon ◽  
Laurent Baricault ◽  
Nicole Gas ◽  
Emmanuelle Guillou ◽  
Annie Valette ◽  
...  
Keyword(s):  
Membrane Structure ◽  
Inner Membrane ◽  
Mitochondrial Inner Membrane
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