The plant mitochondrial proteome

Research output: Contribution to journalReview articleResearchpeer review

Authors

  • A. Harvey Millar
  • Joshua L. Heazlewood
  • Brian K. Kristensen
  • Hans Peter Braun
  • Ian M. Møller

Research Organisations

External Research Organisations

  • University of Western Australia
  • Technical University of Denmark
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Details

Original languageEnglish
Pages (from-to)36-43
Number of pages8
JournalTrends in plant science
Volume10
Issue number1
Publication statusPublished - 19 Dec 2004

Abstract

The plant mitochondrial proteome might contain as many as 2000-3000 different gene products, each of which might undergo post-translational modification. Recent studies using analytical methods, such as one-, two- and three-dimensional gel electrophoresis and one- and two-dimensional liquid chromatography linked on-line with tandem mass spectrometry, have identified >400 mitochondrial proteins, including subunits of mitochondrial respiratory complexes, supercomplexes, phosphorylated proteins and oxidized proteins. The results also highlight a range of new mitochondrial proteins, new mitochondrial functions and possible new mechanisms for regulating mitochondrial metabolism. More than 70 identified proteins in Arabidopsis mitochondrial samples lack similarity to any protein of known function. In some cases, unknown proteins were found to form part of protein complexes, which allows a functional context to be defined for them. There are indications that some of these proteins add novel activities to mitochondrial protein complexes in plants.

ASJC Scopus subject areas

Cite this

The plant mitochondrial proteome. / Millar, A. Harvey; Heazlewood, Joshua L.; Kristensen, Brian K. et al.
In: Trends in plant science, Vol. 10, No. 1, 19.12.2004, p. 36-43.

Research output: Contribution to journalReview articleResearchpeer review

Millar, AH, Heazlewood, JL, Kristensen, BK, Braun, HP & Møller, IM 2004, 'The plant mitochondrial proteome', Trends in plant science, vol. 10, no. 1, pp. 36-43. https://doi.org/10.1016/j.tplants.2004.12.002
Millar, A. H., Heazlewood, J. L., Kristensen, B. K., Braun, H. P., & Møller, I. M. (2004). The plant mitochondrial proteome. Trends in plant science, 10(1), 36-43. https://doi.org/10.1016/j.tplants.2004.12.002
Millar AH, Heazlewood JL, Kristensen BK, Braun HP, Møller IM. The plant mitochondrial proteome. Trends in plant science. 2004 Dec 19;10(1):36-43. doi: 10.1016/j.tplants.2004.12.002
Millar, A. Harvey ; Heazlewood, Joshua L. ; Kristensen, Brian K. et al. / The plant mitochondrial proteome. In: Trends in plant science. 2004 ; Vol. 10, No. 1. pp. 36-43.
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title = "The plant mitochondrial proteome",
abstract = "The plant mitochondrial proteome might contain as many as 2000-3000 different gene products, each of which might undergo post-translational modification. Recent studies using analytical methods, such as one-, two- and three-dimensional gel electrophoresis and one- and two-dimensional liquid chromatography linked on-line with tandem mass spectrometry, have identified >400 mitochondrial proteins, including subunits of mitochondrial respiratory complexes, supercomplexes, phosphorylated proteins and oxidized proteins. The results also highlight a range of new mitochondrial proteins, new mitochondrial functions and possible new mechanisms for regulating mitochondrial metabolism. More than 70 identified proteins in Arabidopsis mitochondrial samples lack similarity to any protein of known function. In some cases, unknown proteins were found to form part of protein complexes, which allows a functional context to be defined for them. There are indications that some of these proteins add novel activities to mitochondrial protein complexes in plants.",
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AU - Heazlewood, Joshua L.

AU - Kristensen, Brian K.

AU - Braun, Hans Peter

AU - Møller, Ian M.

N1 - Funding information: We thank the following agencies for financial support – The Danish Agricultural and Veterinary Research Council and the Danish Natural Science Research Council (I.M.M.), the Australian Research Council Discovery Programme (A.H.M.), The University of Western Australia (A.H.M. and J.L.H.) and the Deutsche Forschungsgemeinschaft (H-P.B.).

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