Export of Proteins from Mitochondria

Autor: Robert O. Poyton, Edward E. McKee, Vicki Cameron, Bradley Goehring, Kevin A. Sevarino, David J.M. Duhl
Rok vydání: 1996
Předmět:
DOI: 10.1016/s1569-2558(09)60017-5
Popis: Publisher Summary This chapter discusses the protein export, and its relationship(s) to the other transport pathways of mitochondria. Nuclear gene products are exported from the mitochondrial matrix to the inner membrane space by a process termed “conservative sorting.” Proteins that follow this pathway are translated in the cytosol and localized to the matrix by standard import pathways. Nuclear gene products may also be released from the mitochondrial matrix or intermembrane space into the cytosol. Thus, nuclear gene products may be exported to either the intermembrane space or to the cytosol. Several lines of evidence indicate that mitochondrially-encoded proteins are inserted into the inner mitochondrial membrane co-translationally. The most direct evidence comes from studies with cytochrome c oxidase presubunit II in yeast. The leader peptide of this preprotein is processed by Implp, which is located on the external surface of the inner membrane. Hence, processing is a convenient measure of insertion because the precursor becomes accessible to the protease only after its insertion into the inner membrane. Because presubunit II is processed co-translationally, it follows that it is also inserted into the membrane co-translationally.
Databáze: OpenAIRE