Processing of precursor proteins by plant mitochondria.
Precursor proteins from Neurospora crassa were correctly processed by a matrix extract from Vicia faba and cauliflower mitochondria. Processing yielded mature protein of the same molecular mass as mature Neurospora protein. The processing activity has two components. One is antigenically related to and of the same molecular mass as the processing enhancing protein of Neurospora. The second component was not recognized by antibody to the matrix processing protease from Neurospora mitochondria. The second component also houses the protease activity. Similar results were obtained using precursors to both the F1 beta subunit of the mitochondrial F0F1 ATPase and subunit V of the Rieske FeS complex from Neurospora. The beta subunit of the F0F1 ATPASE was processed to the mature form. Subunit V of the Rieske FeS complex was processed to the intermediate form only. Additional processing seen during import into plant mitochondria is not catalyzed by these proteins.
Whelan
J
J
Department of Botany, University College Dublin, Belfield, Ireland.
O'Mahony
P
P
Harmey
M A
MA
D015153:Blotting, Western; D066298:In Vitro Techniques; D007506:Iron-Sulfur Proteins / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism*; D008970:Molecular Weight; D009492:Neurospora crassa; D010447:Peptide Hydrolases / Q000378:metabolism; D010940:Plant Proteins / Q000378:metabolism*; D011498:Protein Precursors / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D006180:Proton-Translocating ATPases / Q000378:metabolism
D007506:Iron-Sulfur Proteins; D010940:Plant Proteins; D011498:Protein Precursors; D010447:Peptide Hydrolases; D006180:Proton-Translocating ATPases