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Tufm encodes a protein which participates in protein translation in mitochondria. Additionally we are shipping Tu Translation Elongation Factor, Mitochondrial Antibodies (66) and Tu Translation Elongation Factor, Mitochondrial Kits (6) and many more products for this protein.
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we identify a novel signaling hub centering on the NLRX1 TUFM protein complex, promoting autophagic flux. Defects in the expression of either NLRX1 or TUFM result in compromised autophagy when treated with EGFR (show EGFR Proteins) inhibitors.These findings expand our understanding of the components involved in head and neck squamous cell carcinoma autophagy machinery that responds to EGFR (show EGFR Proteins) inhibitors.
TUFM is a novel regulator of epithelial-mesenchymal transition (EMT (show ITK Proteins)); there may be a molecular link between mitochondrial dysfunction and EMT (show ITK Proteins) induction
NLRX1 and TUFM work in concert to reduce cytokine response and augment autophagy.
Increased expression of TUFM is a promising new prognostic indicator for colorectal carcinoma.
By recruiting Atg5 (show ATG5 Proteins)-Atg12 (show ATG12 Proteins) and NLRX1, TUFM serves as a nodal checkpoint of the RIG-I (show DDX58 Proteins)-MAVS (show MAVS Proteins) axis. It acts similarly to NLRX1 by inhibiting RigI (show DDX58 Proteins)-like-receptor-induced IFN-I but promoting autophagy.
Genetic investigation of patients with defective mitochondrial translation led to the discovery of novel mutations in the mitochondrial elongation factor G1 (EFG1 (show GFM1 Proteins)) in one affected baby and in the mitochondrial elongation factor Tu (show EEF1A1 Proteins) (EFTu) in another one
Myoblasts isolated from the MELAS patients show A3243G mutation in tRNALeu(UUR) produces a severe respiratory chain deficiency and this phenotype can be partially suppressed by overexpression of EFTu and EFG2 (show GFM2 Proteins).
Results suggest that the R336Q mutant mt-EFTu variant fails to bind to aminoacylated mitochondrial tRNAs, thus explaining the observed impairment of mitochondrial translation.
Loss of activity is caused by a significant reduction in the ability of EF-Ts (show TSFM Proteins)(mt) R325W to bind EF-Tu(mt), leading to a defect in nucleotide exchange.
Recombinant mitochondrial EF-Tu prevents thermal aggregation of proteins and enhances protein refolding in vitro.
The arginine residue at position 335 of bovine mitochondrial elongation factor Tu (EF-Tu (show EEF1A1 Proteins)) plays an important role in the binding and EF-Tu-mediated delivery of mitochondrial aminoacyl-tRNAs to the A-site of the ribosome.
This gene encodes a protein which participates in protein translation in mitochondria. Mutations in this gene have been associated with combined oxidative phosphorylation deficiency resulting in lactic acidosis and fatal encephalopathy. A pseudogene has been identified on chromosome 17.
Tu translation elongation factor, mitochondrial
, elongation factor Tu, mitochondrial-like
, elongation factor Tu, mitochondrial