scholarly journals Nuclear respiratory factor 2 induces SIRT 3 expression

Aging Cell ◽  
2015 ◽  
Vol 14 (5) ◽  
pp. 818-825 ◽  
Author(s):  
F. Kyle Satterstrom ◽  
William R. Swindell ◽  
Gaëlle Laurent ◽  
Sejal Vyas ◽  
Martha L. Bulyk ◽  
...  
Keyword(s):  
Nuclear Respiratory Factor ◽  
Nuclear Respiratory Factor 2

scholarly journals Four structurally distinct, non-DNA-binding subunits of human nuclear respiratory factor 2 share a conserved transcriptional activation domain.

1995 ◽  
Vol 15 (1) ◽  
pp. 102-111 ◽  
Author(s):  
S Gugneja ◽  
J V Virbasius ◽  
R C Scarpulla
Keyword(s):  
Dna Binding ◽  
Protein Interactions ◽  
Transcriptional Activation ◽  
Deletion Mapping ◽  
Rnase Protection ◽  
Nuclear Respiratory Factor ◽  
Gamma Subunits ◽  
Nuclear Respiratory Factor 2 ◽  
Alpha Beta ◽  
Beta 2

Nuclear respiratory factor 2 (NRF-2) was previously purified to near homogeneity from HeLa cells on the basis of its ability to bind tandem recognition sites in the rat cytochrome oxidase subunit IV (RCO4) promoter. It consisted of five subunits, alpha, beta 1, beta 2, gamma 1, and gamma 2. Sequencing of tryptic peptides from alpha and from mixtures of the two beta or two gamma subunits revealed sequence identities with subunits of the mouse GA-binding protein (GABP), a ubiquitously expressed ETS domain activator composed of three subunits, alpha, beta 1, and beta 2. To understand the precise relationship between NRF-2 and GABP, cDNAs for all five NRF-2 subunits have now been cloned and their products have been overexpressed. The results establish that the two additional NRF-2 subunits are molecular variants that differ from GABP beta 1 and beta 2 by having a 12-amino-acid insertion containing two serine doublets. PCR and RNase protection assays show that mRNAs for these variants are expressed in the human but not the rodent cells and tissues examined. The insertion did not alter the ability of the beta and gamma subunits to associate with alpha, the DNA-binding subunit, nor did it affect the ability of NRF-2 beta 1 or beta 2 to direct high-affinity binding of alpha to tandem sites in the RCO4 promoter. In addition, the four NRF-2 beta and gamma subunits were equally proficient in activating transcription in transfected cells when fused to a GAL4 DNA-binding domain. The domain responsible for this transcriptional activation was localized by deletion mapping to a region of approximately 70 amino acids that is conserved in all four NRF-2 beta and gamma subunits. The repeated glutamine-containing hydrophobic clusters within this region bear a strong resemblance to those recently implicated in protein-protein interactions within the transcriptional apparatus.

scholarly journals Intellectual disability-associated factor Zbtb11 cooperates with NRF-2/GABP to control mitochondrial function

2019 ◽  
Author(s):  
Brooke C. Wilson ◽  
Lena Boehme ◽  
Ambra Annibali ◽  
Alan Hodgkinson ◽  
Thomas S. Carroll ◽  
...  
Keyword(s):  
Intellectual Disability ◽  
Mitochondrial Function ◽  
Complex I ◽  
Target Genes ◽  
Cellular Functions ◽  
Experimental Modelling ◽  
Nuclear Respiratory Factor ◽  
Nuclear Respiratory Factor 2 ◽  
Respiratory Complex I ◽  
Complex I Assembly

AbstractZbtb11 is a conserved transcription factor mutated in families with hereditary intellectual disability. Its precise molecular and cellular functions are currently unknown, precluding our understanding of the aetiology of this disease. Using a combination of functional genomics, genetic and biochemical approaches here we show that Zbtb11 plays essential roles in maintaining the homeostasis of mitochondrial function. Mechanistically, we find Zbtb11 facilitates the recruitment of Nuclear Respiratory Factor 2 (NRF-2) to its target promoters, activating a subset of nuclear genes with roles in the biogenesis of respiratory complex I and the mitoribosome. Genetic inactivation of Zbtb11 resulted in a severe complex I assembly defect, impaired mitochondrial respiration, mitochondrial depolarisation, and ultimately proliferation arrest and cell death. Experimental modelling of the pathogenic human mutations showed these have a destabilising effect on the protein, resulting in reduced Zbtb11 dosage, down-regulation of its target genes, and impaired complex I biogenesis. Our study establishes Zbtb11 as a novel essential mitochondrial regulator, improves our understanding of the transcriptional mechanisms of nuclear control over mitochondria, and provides a rationale for the aetiology of Zbtb11-associated intellectual disability.

scholarly journals Thyroid hormone increases transcription of GA-binding protein/nuclear respiratory factor-2 α-subunit in rat liver

FEBS Letters ◽  
2002 ◽  
Vol 514 (2-3) ◽  
pp. 309-314 ◽  
Author(s):  
Angeles Rodrı́guez-Peña ◽  
Héctor Escrivá ◽  
Ana C Handler ◽  
Carmen G Vallejo
Keyword(s):  
Thyroid Hormone ◽  
Rat Liver ◽  
Binding Protein ◽  
Α Subunit ◽  
Nuclear Respiratory Factor ◽  
Nuclear Respiratory Factor 2 ◽  
Ga Binding Protein
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