The N-terminal region of mature mitochondrial aspartate aminotransferase can direct cytosolic dihydrofolate reductase into mitochondria in vitro.
Two fused genes were constructed which encode for two chimeric proteins in which either 10 or 191 N-terminal amino acids of mature mitochondrial aspartate aminotransferase had been attached to the entire polypeptide chain of cytosolic dihydrofolate reductase. The precursor and mature form of mitochondrial aspartate aminotransferase, dihydrofolate reductase and both chimeric proteins were synthesized in vitro and their import into isolated mitochondria was studied. Both chimeric proteins were taken up by isolated organelles, where they became protease resistant, thus indicating the ability of the N-terminal portion of the mature moiety of the precursor of mitochondrial aspartate aminotransferase to direct cytosolic dihydrofolate reductase into mitochondria.
Centro di Studio sui Mitocondri e Metabolismo Energetico, C.N.R., Bari, Italy.
S
S
Giannattasio
A
A
Azzariti
E
E
Marra
E
E
Quagliariello
D001219:Aspartate Aminotransferases / Q000737:chemistry / Q000378:metabolism*; D002451:Cell Compartmentation; D003600:Cytosol / Q000201:enzymology; D066298:In Vitro Techniques; D008928:Mitochondria / Q000201:enzymology*; D011993:Recombinant Fusion Proteins; D013329:Structure-Activity Relationship; D013762:Tetrahydrofolate Dehydrogenase / Q000737:chemistry / Q000378:metabolism*
D011993:Recombinant Fusion Proteins; D013762:Tetrahydrofolate Dehydrogenase; D001219:Aspartate Aminotransferases