Distinctive biochemistry in the trypanosome mitochondrial intermembrane space suggests a model for stepwise evolution of the MIA pathway for import of cysteine-rich proteins

James W.A. Allen, Stuart J. Ferguson, Michael L. Ginger

Research output: Contribution to journalArticle

39 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)2817-2825
Number of pages9
JournalFEBS Letters
Volume582
Issue number19
DOIs
Publication statusPublished - 20 Aug 2008
Externally publishedYes

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Biochemistry
Trypanosomiasis
Electron Transport
Disulfides
Cysteine
Cytology
Protozoa
Mitochondrial Proteins
Substrates
Oxidants
Yeast
Cell Biology
Parasites
Animals
Proteins
Yeasts
Electrons
sulfhydryl oxidase

Cite this

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abstract = "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.",
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Distinctive biochemistry in the trypanosome mitochondrial intermembrane space suggests a model for stepwise evolution of the MIA pathway for import of cysteine-rich proteins. / Allen, James W.A.; Ferguson, Stuart J.; Ginger, Michael L.

In: FEBS Letters, Vol. 582, No. 19, 20.08.2008, p. 2817-2825.

Research output: Contribution to journalArticle

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