A novel extranuclear mutant of Neurospora with a temperature-sensitive defect in mitochondrial protein synthesis and mitochondrial ATPase

1981 ◽  
Vol 181 (1) ◽  
pp. 13-19 ◽  
Author(s):  
Richard A. Collins ◽  
Helmut Bertrand ◽  
Robert J. LaPolla ◽  
Alan M. Lambowitz
Keyword(s):  
Protein Synthesis ◽  
Mitochondrial Protein ◽  
Temperature Sensitive ◽  
Mitochondrial Atpase ◽  
Mitochondrial Protein Synthesis

scholarly journals Bovine mitochondrial protein synthesis elongation factors

1989 ◽  
Vol 264 (32) ◽  
pp. 19125-19131
Author(s):  
C J Schwartzbach ◽  
L L Spremulli
Keyword(s):  
Protein Synthesis ◽  
Mitochondrial Protein ◽  
Mitochondrial Protein Synthesis ◽  
Elongation Factors

scholarly journals Exploring the Ability of LARS2 Carboxy-Terminal Domain in Rescuing the MELAS Phenotype

Life ◽  
2021 ◽  
Vol 11 (7) ◽  
pp. 674
Author(s):  
Francesco Capriglia ◽  
Francesca Rizzo ◽  
Giuseppe Petrosillo ◽  
Veronica Morea ◽  
Giulia d’Amati ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Molecular Mechanisms ◽  
Mitochondrial Protein ◽  
Trna Synthetase ◽  
Mitochondrial Protein Synthesis ◽  
Mitochondrial Translation ◽  
Terminal Domain ◽  
Carboxy Terminal Domain ◽  
Mitochondrial Functions ◽  
Carboxy Terminal

The m.3243A>G mutation within the mitochondrial mt-tRNALeu(UUR) gene is the most prevalent variant linked to mitochondrial encephalopathy with lactic acidosis and stroke-like episodes (MELAS) syndrome. This pathogenic mutation causes severe impairment of mitochondrial protein synthesis due to alterations of the mutated tRNA, such as reduced aminoacylation and a lack of post-transcriptional modification. In transmitochondrial cybrids, overexpression of human mitochondrial leucyl-tRNA synthetase (LARS2) has proven effective in rescuing the phenotype associated with m.3243A>G substitution. The rescuing activity resides in the carboxy-terminal domain (Cterm) of the enzyme; however, the precise molecular mechanisms underlying this process have not been fully elucidated. To deepen our knowledge on the rescuing mechanisms, we demonstrated the interactions of the Cterm with mutated mt-tRNALeu(UUR) and its precursor in MELAS cybrids. Further, the effect of Cterm expression on mitochondrial functions was evaluated. We found that Cterm ameliorates de novo mitochondrial protein synthesis, whilst it has no effect on mt-tRNALeu(UUR) steady-state levels and aminoacylation. Despite the complete recovery of cell viability and the increase in mitochondrial translation, Cterm-overexpressing cybrids were not able to recover bioenergetic competence. These data suggest that, in our MELAS cell model, the beneficial effect of Cterm may be mediated by factors that are independent of the mitochondrial bioenergetics.

The effect of inhibition of mitochondrial protein synthesis on the proliferation and phenotypic properties of a rat leukemia in different stages of in-vivo tumor development

1987 ◽  
Vol 11 (6) ◽  
pp. 529-536 ◽  
Author(s):  
Coby Van den Bogert ◽  
Bert H.J. Dontje ◽  
Štefan Kuẑela ◽  
Trudi E. Melis ◽  
Davine Opstelten ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Mitochondrial Protein ◽  
Tumor Development ◽  
Mitochondrial Protein Synthesis ◽  
Phenotypic Properties
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