Partitioning of Malate Dehydrogenase Isoenzymes into Glyoxysomes, Mitochondria, and Chloroplasts
- 1 October 1992
- journal article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 100 (2) , 557-559
- https://doi.org/10.1104/pp.100.2.557
Abstract
Malate dehydrogenase isoenzymes catalyzing the oxidation of malate to oxaloacetate are highly active enzymes in mitochondria, in peroxisomes, in chloroplasts, and in the cytosol. Determination of the primary structure of the isoenzymes has disclosed that they are encoded in different nuclear genes. All three organelle-targeted malate dehydrogenases are synthesized with an amino terminal extension that is cleaved off in connection with the import of the enzyme precursor into the organelle. The sequence of the 27 amino acids of the mitochondrial transit peptide is unrelated to the 37-residue glyoxysomal transit peptide, which in turn is entirely different in sequence from the 57-residue chloroplastic transit peptide. With the exception of malate dehydrogenase and 3-ketoacyl thiolase, peroxisomal enzymes are synthesized without transit peptides and are frequently translocated into the organelle with a peroxisomal targeting signal consisting of a conserved tripeptide at the carboxy terminus of the protein. Based on the observation that this tripeptide (Ala-His-Leu) occurs in the transit peptides of glyoxysomal malate dehydrogenase and peroxisomal 3-ketoacyl thiolase, the possible significance of amino terminal transit peptides for peroxisome import is discussed.Keywords
This publication has 7 references indexed in Scilit:
- Mistargeting of peroxisomal L-alanine:glyoxylate aminotransferase to mitochondria in primary hyperoxaluria patients depends upon activation of a cryptic mitochondrial targeting sequence by a point mutation.Proceedings of the National Academy of Sciences, 1991
- Evolutionary conservation of a microbody targeting signal that targets proteins to peroxisomes, glyoxysomes, and glycosomes.The Journal of cell biology, 1991
- Glyoxysomal malate dehydrogenase from watermelon is synthesized with an amino-terminal transit peptide.Proceedings of the National Academy of Sciences, 1990
- Mitochondrial malate dehydrogenase from watermelon: sequence of cDNA clones and primary structure of the higher-plant precursor proteinPlant Molecular Biology, 1990
- A single amino acid substitution in lactate dehydrogenase improves the catalytic efficiency with an alternative coenzymeBiochemical and Biophysical Research Communications, 1990
- A conserved tripeptide sorts proteins to peroxisomes.The Journal of cell biology, 1989
- STRUCTURAL-ANALYSIS OF CDNA FOR RAT PEROXISOMAL 3-KETOACYL-COA THIOLASE1987