Allen, James W.A., Ferguson, Stuart J. and Ginger, Michael L. (2008) Distinctive biochemistry in the trypanosome mitochondrial intermembrane space suggests a model for stepwise evolution of the MIA pathway for import of cysteine-rich proteins. FEBS Letters, 582 (19). pp. 2817-2825. ISSN 0014-5793Metadata only available from this repository.
Mia40-dependent disulphide bond exchange is used by animals, yeast, and probably plants for import of small, cysteine-rich proteins into the mitochondrial intermembrane space (IMS). During import, electrons are transferred from the imported substrate to Mia40 then, via the sulphydryl oxidase Erv1, into the respiratory chain. Curiously, however, there are protozoa which contain substrates for Mia40-dependent import, but lack Mia40. There are also organisms where Erv1 is present in the absence of respiratory chain components. In accommodating these and other relevant observations pertaining to mitochondrial cell biology, we hypothesise that the ancestral IMS import pathway for disulphide-bonded proteins required only Erv1 (but not Mia40) and identify parasites in which O2 is the likely physiological oxidant for Erv1.
|Subjects:||Q Science > QH Natural history > QH301 Biology|
|Schools:||School of Applied Sciences|
|Depositing User:||Michael Ginger|
|Date Deposited:||10 May 2016 08:14|
|Last Modified:||10 May 2016 08:14|
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