AI Article Synopsis
- Mohr-Tranebjaerg syndrome (MTS) is a neurodegenerative disorder leading to hearing loss, dystonia, mental retardation, and blindness, caused by mutations in the DDP1 gene.
- DDP1 is similar to yeast proteins involved in the mitochondrial import machinery, indicating its role in mitochondrial function.
- Research identified six additional human genes related to DDP1, suggesting potential links to other neurodegenerative diseases.
Article Abstract
The Mohr-Tranebjaerg syndrome (MTS), a neurodegenerative syndrome characterized by progressive sensorineural hearing loss, dystonia, mental retardation and blindness, is a mitochondrial disease caused by mutations in the deafness/dystonia peptide 1 (DDP1) gene. DDP1 shows similarity to the yeast proteins Tim9, Tim10 and Tim12, components of the mitochondrial import machinery for carrier proteins. Here, we show that DDP1 belongs to a large family of evolutionarily conserved proteins. We report the identification, chromosomal localization and expressional analysis of six human family members which represent further candidate genes for neurodegenerative diseases.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/s0014-5793(99)01665-8 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Novel c.221+1dup pathogenic variant in AGK gene linked to Sengers syndrome.
Neuromuscul Disord
December 2024
University of Florida College of Medicine - Jacksonville, Jacksonville, FL, USA.
Sengers Syndrome (SS) is a rare autosomal recessive mitochondrial disorder caused by mutations in the acylglycerol kinase (AGK) gene on chromosome 7, also known as cardiomyopathic mitochondrial DNA depletion syndrome (MTDPS10). This disorder disrupts mitochondrial DNA function and energy metabolism, presenting with symptoms such as congenital cataracts, hypertrophic cardiomyopathy, skeletal myopathy, exercise intolerance, and lactic acidosis. Previous research has shown SS affects oxidative phosphorylation and mitochondrial respiration, implicating the TIM22 complex and carrier import.
View Article and Find Full Text PDFDbi1 is an oxidoreductase and an assembly chaperone for mitochondrial inner membrane proteins.
EMBO Rep
January 2025
LMU Munich, Biozentrum-Cell Biology, 82152, Planegg-Martinsried, Germany.
Import and assembly of mitochondrial proteins into multimeric complexes are essential for cellular function. Yet, many steps of these processes and the proteins involved remain unknown. Here, we identify a novel pathway for disulfide bond formation and assembly of mitochondrial inner membrane (IM) proteins.
View Article and Find Full Text PDFAnalysis of mitochondrial translocases TOM and TIM by the patch-clamping technique.
Methods Enzymol
November 2024
Department of Biochemistry and Molecular Biology, and Genetics, Faculty of Veterinary Sciences, University of Extremadura, Cáceres, Spain. Electronic address:
Mitochondrial protein import and sorting relies on sophisticated molecular machineries or translocases, of which channels are integral. Channels are built upon membrane proteins whose functions are driven by conformational changes. This implies that structural and functional information need to be integrated to gain a deep understanding of their dynamic behavior.
View Article and Find Full Text PDFThe MitoLuc assay for the analysis of the mechanism of mitochondrial protein import.
Methods Enzymol
October 2024
School of Biochemistry, University of Bristol, Bristol, United Kingdom. Electronic address:
The NanoLuc split luciferase assay has proven to be a powerful tool for the analysis of protein translocation. Its flexibility has enabled in vivo, ex vivo, and in vitro studies-including systems reconstituting protein transport from pure components. The assay has been particularly useful in the characterization of bacterial secretion and mitochondrial protein import.
View Article and Find Full Text PDFRole of Yme1 in mitochondrial protein homeostasis: from regulation of protein import, OXPHOS function to lipid synthesis and mitochondrial dynamics.
Biochem Soc Trans
June 2024
School of Biological Sciences, Faculty of Biology, Medicine and Health, Manchester Academic Health Science Centre, The University of Manchester, Manchester M13 9PT, U.K.
Mitochondria are essential organelles of eukaryotic cells and thus mitochondrial proteome is under constant quality control and remodelling. Yme1 is a multi-functional protein and subunit of the homo-hexametric complex i-AAA proteinase. Yme1 plays vital roles in the regulation of mitochondrial protein homeostasis and mitochondrial plasticity, ranging from substrate degradation to the regulation of protein functions involved in mitochondrial protein biosynthesis, energy production, mitochondrial dynamics, and lipid biosynthesis and signalling.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!