scholarly journals Erratum: Corrigendum: Human Mitochondrial DNA-Protein Complexes Attach to a Cholesterol-Rich Membrane Structure

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Joachim M. Gerhold ◽  
Şirin Cansiz-Arda ◽  
Madis Lõhmus ◽  
Oskar Engberg ◽  
Aurelio Reyes ◽  
...  
Keyword(s):  
Mitochondrial Dna ◽  
Membrane Structure ◽  
Protein Complexes ◽  
Human Mitochondrial Dna

scholarly journals Human Mitochondrial DNA-Protein Complexes Attach to a Cholesterol-Rich Membrane Structure

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Joachim M. Gerhold ◽  
Şirin Cansiz-Arda ◽  
Madis Lõhmus ◽  
Oskar Engberg ◽  
Aurelio Reyes ◽  
...  
Keyword(s):  
Membrane Structure ◽  
Protein Complexes ◽  
Cholesterol Homeostasis ◽  
Membrane Composition ◽  
Human Mitochondrial Dna ◽  
Associated Proteins ◽  
Mtdna Replication ◽  
Mitochondrial Cholesterol ◽  
Mitochondrial Junctions ◽  
Mitochondrial Lipids

Abstract The helicase Twinkle is indispensable for mtDNA replication in nucleoids. Previously, we showed that Twinkle is tightly membrane-associated even in the absence of mtDNA, which suggests that Twinkle is part of a membrane-attached replication platform. Here we show that this platform is a cholesterol-rich membrane structure. We fractionated mitochondrial membrane preparations on flotation gradients and show that membrane-associated nucleoids accumulate at the top of the gradient. This fraction was shown to be highly enriched in cholesterol, a lipid that is otherwise low abundant in mitochondria. In contrast, more common mitochondrial lipids and abundant inner-membrane associated proteins concentrated in the bottom-half of these gradients. Gene silencing of ATAD3, a protein with proposed functions related to nucleoid and mitochondrial cholesterol homeostasis, modified the distribution of cholesterol and nucleoids in the gradient in an identical fashion. Both cholesterol and ATAD3 were previously shown to be enriched in ER-mitochondrial junctions and we detect nucleoid components in biochemical isolates of these structures. Our data suggest an uncommon membrane composition that accommodates platforms for replicating mtDNA and reconcile apparently disparate functions of ATAD3. We suggest that mtDNA replication platforms are organized in connection with ER-mitochondrial junctions, facilitated by a specialized membrane architecture involving mitochondrial cholesterol.

Geographic Origin of Human Mitochondrial DNA Revisited

1992 ◽  
Vol 41 (3) ◽  
pp. 384-391 ◽  
Author(s):  
M. Stoneking ◽  
S. T. Sherry ◽  
L. Vigilant
Keyword(s):  
Mitochondrial Dna ◽  
Geographic Origin ◽  
Human Mitochondrial Dna

Human Mitochondrial DNA Polymerase Holoenzyme: Reconstitution and Characterization†

Biochemistry ◽  
2000 ◽  
Vol 39 (7) ◽  
pp. 1702-1708 ◽  
Author(s):  
Allison A. Johnson ◽  
Yu-chih Tsai ◽  
Steven W. Graves ◽  
Kenneth A. Johnson
Keyword(s):  
Mitochondrial Dna ◽  
Dna Polymerase ◽  
Human Mitochondrial Dna ◽  
Mitochondrial Dna Polymerase

scholarly journals Modular Architecture of the Hexameric Human Mitochondrial DNA Helicase

2007 ◽  
Vol 367 (5) ◽  
pp. 1382-1391 ◽  
Author(s):  
Tawn D. Ziebarth ◽  
Carol L. Farr ◽  
Laurie S. Kaguni
Keyword(s):  
Mitochondrial Dna ◽  
Dna Helicase ◽  
Modular Architecture ◽  
Human Mitochondrial Dna

Assignment of two mitochondrially synthesized polypeptides to human mitochondrial DNA and their use in the study of intracellular mitochondrial interaction

1982 ◽  
Vol 2 (1) ◽  
pp. 30-41
Author(s):  
N A Oliver ◽  
D C Wallace
Keyword(s):  
Mitochondrial Dna ◽  
Restriction Site ◽  
Mitochondrial Protein ◽  
Mitochondrial Protein Synthesis ◽  
Human Mitochondrial Dna ◽  
Ht1080 Cells ◽  
Mitochondrial Dnas ◽  
A Cell ◽  
Dna Restriction ◽  
Restriction Site Polymorphisms

Two mitochondrially synthesized marker polypeptides, MV-1 and MV-2, were found in human HeLa and HT1080 cells. These were assigned to the mitochondrial DNA in HeLa-HT1080 cybrids and hybrids by demonstrating their linkage to cytoplasmic genetic markers. These markers include mitochondrial DNA restriction site polymorphisms and resistance to chloramphenicol, an inhibitor of mitochondrial protein synthesis. In the absence of chloramphenicol, the expression of MV-1 and MV-2 in cybrids and hybrids was found to be directly proportional to the ratio of the parental mitochondrial DNAs. In the presence of chloramphenicol, the marker polypeptide linked to the chloramphenicol-sensitive mitochondrial DNA continued to be expressed. This demonstrated that resistant and sensitive mitochondrial DNAs can cooperate within a cell for gene expression and that the CAP-resistant allele was dominant or codominant to sensitive. Such cooperation suggests that mitochondrial DNAs can be exchanged between mitochondria.

Atypical clinical presentations associated with the MELAS mutation at position 3243 of human mitochondrial DNA

1993 ◽  
Vol 3 (1) ◽  
pp. 43-50 ◽  
Author(s):  
Carlos T. Moraes ◽  
Federica Ciacci ◽  
Gabriella Silvestri ◽  
Sara Shanske ◽  
Monica Sciacco ◽  
...  
Keyword(s):  
Mitochondrial Dna ◽  
Human Mitochondrial Dna ◽  
Clinical Presentations
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