Valens M, Rinaldi T, Daignan-Fornier B, Bolotin-Fukuhara M
Laboratoire de génétique moléculaire, institut de génétique et microbiologie associé au CNRS, université Paris, Orsay, France.
Biochimie. 1991 Dec;73(12):1525-32. doi: 10.1016/0300-9084(91)90187-6.
The mitochondrial protein synthesis presents specific features and uses specific components different from their cytoplasmic counterparts. Since most genes which code for these components are localized in the chromosomes and only a small number are encoded by the mitochondrial DNA, it is important to identify and characterize the nuclear genes involved in this process. In order to do this, we have used a genetic screening which implies the selection and study of nuclear suppressors of mitochondrial mutations (or the reverse situation) which affect the mitochondrial protein synthesis. Three mutations have been used for this purpose. Two of them (ts 1398, cs 909) impair the mitochondrial ribosome; they were used to characterize new interacting components as well as two genes, MBR1 and MBR2, which control the assembly or the regulation of other genes involved in mitochondrial protein synthesis. The third mutation (ts 932), blocks the 3'-end maturation of the mitochondrial aspartyl tRNA. A nuclear suppressor has been obtained which presents all the characteristics of a mutation in the gene encoding the enzyme responsible for this process.
