Nuclear MRP genes and mitochondrial disease

O’Brien, Thomas W.; O'Brien, B; Norman, Ryan A.

doi:10.1016/j.gene.2005.03.026

Cited by 71 publications

(54 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…For example, the Nudix domain in MRPL46 is also found in decapping enzymes, ADP ribose diphosphatase, and similar proteins, and the double-stranded (ds) RNA-binding protein domain found in MRPL44 and MRPS5 is a generic RNA-binding domain found in diverse enzymes, such as RNA helicases, dsRNA-dependent protein kinase, RNase III, and so forth. The accessory proteins, which are situated on the surface of the ribosome, have been suggested to be involved in cotranslational processes and programmed cell death (42,43), providing examples of how the eukaryotic cell controls the mitochondrial processes.…”

Section: Discussionmentioning

confidence: 99%

Mitochondrial genomes are retained by selective constraints on protein targeting

Björkholm

Harish

Hagström

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Mitochondria are energy-producing organelles in eukaryotic cells considered to be of bacterial origin. The mitochondrial genome has evolved under selection for minimization of gene content, yet it is not known why not all mitochondrial genes have been transferred to the nuclear genome. Here, we predict that hydrophobic membrane proteins encoded by the mitochondrial genomes would be recognized by the signal recognition particle and targeted to the endoplasmic reticulum if they were nuclear-encoded and translated in the cytoplasm. Expression of the mitochondrially encoded proteins Cytochrome oxidase subunit 1, Apocytochrome b, and ATP synthase subunit 6 in the cytoplasm of HeLa cells confirms export to the endoplasmic reticulum. To examine the extent to which the mitochondrial proteome is driven by selective constraints within the eukaryotic cell, we investigated the occurrence of mitochondrial protein domains in bacteria and eukaryotes. The accessory protein domains of the oxidative phosphorylation system are unique to mitochondria, indicating the evolution of new protein folds. Most of the identified domains in the accessory proteins of the ribosome are also found in eukaryotic proteins of other functions and locations. Overall, one-third of the protein domains identified in mitochondrial proteins are only rarely found in bacteria. We conclude that the mitochondrial genome has been maintained to ensure the correct localization of highly hydrophobic membrane proteins. Taken together, the results suggest that selective constraints on the eukaryotic cell have played a major role in modulating the evolution of the mitochondrial genome and proteome. mitochondria | protein domain | evolution | endoplasmatic reticulum | signal recognition particle

show abstract

Section: Discussionmentioning

confidence: 99%

Mitochondrial genomes are retained by selective constraints on protein targeting

Björkholm

Harish

Hagström

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…The death-associated protein 3 (DAP3) is one of the constituents of the small subunit of the mitochondrial ribosome that has no counterpart in bacterial or cytoplasmic ribosomes (Cavdar Koc et al, 2001aSuzuki et al, 2001aSuzuki et al, , 2001bO'Brien et al, 2005). Multiple roles have been assigned to DAP3; first identified as a pro-apoptotic factor, this protein is suspected of interacting with the TNF-related apoptosis-inducing ligand (TRAIL) receptors and the Fas-associated death domain protein (FADD) in the cytosol (Kissil et al, 1995(Kissil et al, , 1999Miyazaki and Reed, 2001).…”

mentioning

confidence: 99%

Death-associated protein 3 is overexpressed in human thyroid oncocytic tumours

et al. 2009

View full text Add to dashboard Cite

BACKGROUND: The human death-associated protein 3 (hDAP3) is a GTP-binding constituent of the small subunit of the mitochondrial ribosome with a pro-apoptotic function. METHODS: A search through publicly available microarray data sets showed 337 genes potentially coregulated with the DAP3 gene. The promoter sequences of these 337 genes and 70 out of 85 mitochondrial ribosome genes were analysed in silico with the DAP3 gene promoter sequence. The mitochondrial role of DAP3 was also investigated in the thyroid tumours presenting various mitochondrial contents. RESULTS: The study revealed nine transcription factors presenting enriched motifs for these gene promoters, five of which are implicated in cellular growth (ELK1, ELK4, RUNX1, HOX11-CTF1, TAL1-ternary complex factor 3) and four in mitochondrial biogenesis (nuclear respiratory factor-1 (NRF-1), GABPA, PPARG-RXRA and estrogen-related receptor alpha (ESRRA)). An independent microarray data set showed the overexpression of ELK1, RUNX1 and ESRRA in the thyroid oncocytic tumours. Exploring the thyroid tumours, we found that DAP3 mRNA and protein expression is upregulated in tumours presenting a mitochondrial biogenesis compared with the normal tissue. ELK1 and ESRRA were also showed upregulated with DAP3. CONCLUSION: ELK1 and ESRRA may be considered as potential regulators of the DAP3 gene expression. DAP3 may participate in mitochondrial maintenance and play a role in the balance between mitochondrial homoeostasis and tumourigenesis.

show abstract

“…Specifically, we postulated that if the heterogeneity within tumors were to be a cumulative effect of genetic drift and amplification of specific stem cell lineages, one would need to define a mechanism for tracing all these in order to resolve their effects at the molecular and cellular level. Mitochondrial genome (mtDNA) analyses, currently applied to study evolutionary history, population migration, forensic medicine (Pakendorf and Stoneking, 2005) and human disease (O'Brien et al, 2005), have been recently applied to model stem cell turnover rates and clonal evolution in normal tissues; hence was thought to be an ideal tool for this study. Among the nuclear genes, the cyclic AMP response element-binding protein (CREBBP) is involved in multiple cellular processes, functions as a transcriptional cofactor and is also a histone acetyltransferase (HAT) (Petrij et al, 1995).…”

Section: Introductionmentioning

confidence: 99%