Abstract
The disulfide relay system found in the intermembrane space (IMS) of mitochondria is an essential pathway for the import and oxidative folding of IMS proteins. Erv1, an essential member of this pathway, has been previously found to be ubiquitously present in mitochondria-containing eukaryotes. However, the other essential protein, Mia40, was found to be absent or not required in some organisms, raising questions about how the disulfide relay functions in these organisms. A recent study published in BMC Biology demonstrates for the first time that some Erv1 proteins can function in oxidative folding independently of a Mia40 protein, providing for the first time strong evidence that the IMS disulfide relay evolved in a stepwise manner.
Item Type: | Journal article |
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Faculties: | Biology > Department Biology I |
Research Centers: | Center for Integrated Protein Science Munich (CIPSM) |
Subjects: | 500 Science > 570 Life sciences; biology 500 Science > 540 Chemistry |
URN: | urn:nbn:de:bvb:19-epub-54524-5 |
ISSN: | 1741-7007 |
Language: | English |
Item ID: | 54524 |
Date Deposited: | 14. Jun 2018, 09:56 |
Last Modified: | 04. Nov 2020, 13:34 |