Home > Research > Publications & Outputs > Distinctive biochemistry in the trypanosome mit...

Research

Links

Text available via DOI:

Keywords

View graph of relations

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

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Published

Standard

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 Journal/Magazine › Journal article › peer-review

Harvard

Allen, JWA, Ferguson, SJ & Ginger, ML 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, vol. 582, no. 19, pp. 2817-2825. https://doi.org/10.1016/j.febslet.2008.07.015

APA

Allen, J. W. A., Ferguson, S. J., & Ginger, M. 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), 2817-2825. https://doi.org/10.1016/j.febslet.2008.07.015

Vancouver

Allen JWA, Ferguson SJ, Ginger ML. 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. 2008 Aug 20;582(19):2817-2825. doi: 10.1016/j.febslet.2008.07.015

Author

Allen, James W. A. ; Ferguson, Stuart J. ; Ginger, Michael L. / Distinctive biochemistry in the trypanosome mitochondrial intermembrane space suggests a model for stepwise evolution of the MIA pathway for import of cysteine-rich proteins. In: FEBS Letters. 2008 ; Vol. 582, No. 19. pp. 2817-2825.

Bibtex

@article{45a1b57582fa4a2981256b0cfa2cd147,
title = "Distinctive biochemistry in the trypanosome mitochondrial intermembrane space suggests a model for stepwise evolution of the MIA pathway for import of cysteine-rich proteins.",
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 O(2) is the likely physiological oxidant for Erv1.",
keywords = "Mitochondria, Disulphide exchange, Mia40, Microsporidia, Evolution, Fe–S cluster, Erv1, Cytochrome c, Trypanosoma",
author = "Allen, {James W. A.} and Ferguson, {Stuart J.} and Ginger, {Michael L.}",
year = "2008",
month = aug,
day = "20",
doi = "10.1016/j.febslet.2008.07.015",
language = "English",
volume = "582",
pages = "2817--2825",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "19",

}

RIS

TY - JOUR

T1 - Distinctive biochemistry in the trypanosome mitochondrial intermembrane space suggests a model for stepwise evolution of the MIA pathway for import of cysteine-rich proteins.

AU - Allen, James W. A.

AU - Ferguson, Stuart J.

AU - Ginger, Michael L.

PY - 2008/8/20

Y1 - 2008/8/20

N2 - 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 O(2) is the likely physiological oxidant for Erv1.

AB - 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 O(2) is the likely physiological oxidant for Erv1.

KW - Mitochondria

KW - Disulphide exchange

KW - Mia40

KW - Microsporidia

KW - Evolution

KW - Fe–S cluster

KW - Erv1

KW - Cytochrome c

KW - Trypanosoma

U2 - 10.1016/j.febslet.2008.07.015

DO - 10.1016/j.febslet.2008.07.015

M3 - Journal article

VL - 582

SP - 2817

EP - 2825

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 19

ER -