A soluble 12-kDa protein of the mitochondrial intermembrane space, Mrs11p, is essential for mitochondrial biogenesis and viability of yeast cells

1997 ◽  
Vol 255 (2) ◽  
pp. 157-165 ◽  
Author(s):  
E. Jarosch ◽  
G. Rödel ◽  
R. J. Schweyen
Keyword(s):  
Mitochondrial Biogenesis ◽  
Yeast Cells ◽  
Intermembrane Space ◽  
Mitochondrial Intermembrane Space

scholarly journals Phosphatidylserine transport by Ups2–Mdm35 in respiration-active mitochondria

2016 ◽  
Vol 214 (1) ◽  
pp. 77-88 ◽  
Author(s):  
Non Miyata ◽  
Yasunori Watanabe ◽  
Yasushi Tamura ◽  
Toshiya Endo ◽  
Osamu Kuge
Keyword(s):  
Yeast Cells ◽  
Intermembrane Space ◽  
Diauxic Shift ◽  
Inner Membrane ◽  
Mitochondrial Inner Membrane ◽  
Mitochondrial Functions ◽  
Phospholipid Transfer ◽  
Metabolic Transition ◽  
Mitochondrial Intermembrane Space

Phosphatidylethanolamine (PE) is an essential phospholipid for mitochondrial functions and is synthesized mainly by phosphatidylserine (PS) decarboxylase at the mitochondrial inner membrane. In Saccharomyces cerevisiae, PS is synthesized in the endoplasmic reticulum (ER), such that mitochondrial PE synthesis requires PS transport from the ER to the mitochondrial inner membrane. Here, we provide evidence that Ups2–Mdm35, a protein complex localized at the mitochondrial intermembrane space, mediates PS transport for PE synthesis in respiration-active mitochondria. UPS2- and MDM35-null mutations greatly attenuated conversion of PS to PE in yeast cells growing logarithmically under nonfermentable conditions, but not fermentable conditions. A recombinant Ups2–Mdm35 fusion protein exhibited phospholipid-transfer activity between liposomes in vitro. Furthermore, UPS2 expression was elevated under nonfermentable conditions and at the diauxic shift, the metabolic transition from glycolysis to oxidative phosphorylation. These results demonstrate that Ups2–Mdm35 functions as a PS transfer protein and enhances mitochondrial PE synthesis in response to the cellular metabolic state.

Mechanisms and physiological impact of the dual localization of mitochondrial intermembrane space proteins

2014 ◽  
Vol 42 (4) ◽  
pp. 952-958 ◽  
Author(s):  
Carmelina Petrungaro ◽  
Jan Riemer
Keyword(s):  
Oxidative Stress ◽  
Mitochondrial Function ◽  
The Other ◽  
Yeast Cells ◽  
Eukaryotic Cells ◽  
Intermembrane Space ◽  
Dual Localization ◽  
Mitochondrial Intermembrane Space ◽  
Physiological Impact ◽  
Cellular Compartments

Eukaryotic cells developed diverse mechanisms to guide proteins to more than one destination within the cell. Recently, the proteome of the IMS (intermembrane space) of mitochondria of yeast cells was identified showing that approximately 20% of all soluble IMS proteins are dually localized to the IMS, as well as to other cellular compartments. Half of these dually localized proteins are important for oxidative stress defence and the other half are involved in energy homoeostasis. In the present review, we discuss the mechanisms leading to the dual localization of IMS proteins and the implications for mitochondrial function.

Conserved substrate binding by chaperones in the bacterial periplasm and the mitochondrial intermembrane space

2007 ◽  
Vol 409 (2) ◽  
pp. 377-387 ◽  
Author(s):  
Felicity H. Alcock ◽  
J. Günter Grossmann ◽  
Ian E. Gentle ◽  
Vladimir A. Likić ◽  
Trevor Lithgow ◽  
...  
Keyword(s):  
Substrate Binding ◽  
Binding Specificity ◽  
Yeast Cells ◽  
Mitochondrial Outer Membrane ◽  
Intermembrane Space ◽  
Hydrophobic Membrane ◽  
Inner Membrane ◽  
Mitochondrial Inner Membrane ◽  
Mitochondrial Intermembrane Space ◽  
Substrate Proteins

Mitochondria were derived from intracellular bacteria and the mitochondrial intermembrane space is topologically equivalent to the bacterial periplasm. Both compartments contain ATP-independent chaperones involved in the transport of hydrophobic membrane proteins. The mitochondrial TIM (translocase of the mitochondrial inner membrane) 10 complex and the periplasmic chaperone SurA were examined in terms of evolutionary relation, structural similarity, substrate binding specificity and their function in transporting polypeptides for insertion into membranes. The two chaperones are evolutionarily unrelated; structurally, they are also distinct both in their characteristics, as determined by SAXS (small-angle X-ray scattering), and in pairwise structural comparison using the distance matrix alignment (DALILite server). Despite their structural differences, SurA and the TIM10 complex share a common binding specificity in Pepscan assays of substrate proteins. Comprehensive analysis of the binding on a total of 1407 immobilized 13-mer peptides revealed that the TIM10 complex, like SurA, does not bind hydrophobic peptides generally, but that both chaperones display selectivity for peptides rich in aromatic residues and with net positive charge. This common binding specificity was not sufficient for SurA to completely replace TIM10 in yeast cells in vivo. In yeast cells lacking TIM10, when SurA is targeted to the intermembrane space of mitochondria, it binds translocating substrate proteins, but fails to completely transfer the substrate to the translocase in the mitochondrial inner membrane. We suggest that SurA was incapable of presenting substrates effectively to the primitive TOM (translocase of the mitochondrial outer membrane) and TIM complexes in early mitochondria, and was replaced by the more effective small Tim chaperone.

scholarly journals Proteomic Mapping of the Human Mitochondrial Intermembrane Space in Live Cells via Ratiometric APEX Tagging

2014 ◽  
Vol 55 (2) ◽  
pp. 332-341 ◽  
Author(s):  
Victoria Hung ◽  
Peng Zou ◽  
Hyun-Woo Rhee ◽  
Namrata D. Udeshi ◽  
Valentin Cracan ◽  
...  
Keyword(s):  
Live Cells ◽  
Intermembrane Space ◽  
Mitochondrial Intermembrane Space

scholarly journals The Mitochondrial Intermembrane Space Oxireductase Mia40 Funnels the Oxidative Folding Pathway of the CytochromecOxidase Assembly Protein Cox19

2014 ◽  
Vol 289 (14) ◽  
pp. 9852-9864 ◽  
Author(s):  
Hugo Fraga ◽  
Joan-Josep Bech-Serra ◽  
Francesc Canals ◽  
Gabriel Ortega ◽  
Oscar Millet ◽  
...  
Keyword(s):  
Folding Pathway ◽  
Intermembrane Space ◽  
Oxidative Folding ◽  
Mitochondrial Intermembrane Space

The Yeast Mitochondrial Intermembrane Space: Purification and Analysis of Two Distinct Fractions

1998 ◽  
Vol 265 (1) ◽  
pp. 123-128 ◽  
Author(s):  
Heiko Martin ◽  
Christoph Eckerskorn ◽  
Frank Gärtner ◽  
Joachim Rassow ◽  
Fritz Lottspeich ◽  
...  
Keyword(s):  
Intermembrane Space ◽  
Mitochondrial Intermembrane Space
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