Biosynthetic pathway of mitochondrial ATPase subunit 9 in Neurospora crassa.
Open Access
- 1 January 1983
- journal article
- research article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 96 (1), 248-255
- https://doi.org/10.1083/jcb.96.1.248
Abstract
Subunit 9 of mitochondrial ATPase (Su9) is synthesized in reticulocyte lysates programmed with Neurospora poly A-RNA, and in a Neurospora cell free system as a precursor with a higher apparent MW than the mature protein (MW 16,400 vs. 10,500). The RNA which directs the synthesis of Su9 precursor is associated with free polysomes. The precursor occurs as a high-MW aggregate in the postribosomal supernatant of reticulocyte lysates. Transfer in vitro of the precursor into isolated mitochondria is demonstrated. This process includes the correct proteolytic cleavage of the precursor to the mature form. After transfer, the protein acquires the following properties of the assembled subunit: it is resistant to added protease, it is soluble in chloroform/methanol, and it can be immunoprecipitated with antibodies to F1-ATPase. The precursor to Su9 is also detected in intact cells after pulse labeling. Processing in vivo takes place post-translationally. It is inhibited by the uncoupler carbonylcyanide m-chlorophenylhdyrazone (CCCP). A hypothetical mechanism is discussed for the intracellular transfer of Su9. It entails synthesis on free polysomes, release of the precursor into the cytosol, recognition by a receptor on the mitochondrial surface and transfer into the inner mitochondrial membrane, which is accompanied by proteolytic cleavage and which depends on an electrical potential across the inner mitochondrial membrane.This publication has 41 references indexed in Scilit:
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