Induction of enzymes of the glycerophosphate pathway in leu-5 mutants of Neurospora crassa.
The inducible cytosolic glycerokinase and mitochondrial glycerol-3-phosphate dehydrogenase have been examined during the glycerol-specific induction in Neurospora crassa. Although both the fully induced levels and the respective rates of synthesis of these two enzymes were less than observed with wild-type cells, there were no major differences in the relative rates of induction of the glycerol-3-phosphate dehydrogenase at either permissive or restrictive temperatures. These results indicate that the processes involved in the assembly of this enzyme into the mitochondrial inner membrane are normal in a mutant lacking the mitochondrial leucyl tRNA synthetase and suggest that the functions of the mitochondrial synthetase may be replaced by those of the cytosolic leucyl tRNA synthetase.
D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D004790:Enzyme Induction; D005991:Glycerol Kinase / Q000096:biosynthesis*; D005993:Glycerolphosphate Dehydrogenase / Q000096:biosynthesis*; D007935:Leucine-tRNA Ligase / Q000378:metabolism*; D008928:Mitochondria / Q000201:enzymology; D009154:Mutation; D009491:Neurospora / Q000201:enzymology*; D009492:Neurospora crassa / Q000201:enzymology*; D010770:Phosphotransferases / Q000096:biosynthesis*
D005993:Glycerolphosphate Dehydrogenase; D010770:Phosphotransferases; D005991:Glycerol Kinase; D000604:Amino Acyl-tRNA Synthetases; D007935:Leucine-tRNA Ligase