The proteome of higher plant mitochondria
- authored by
- R. S.P. Rao, F. Salvato, B. Thal, H. Eubel, J. J. Thelen, I. M. Møller
- Abstract
Plant mitochondria perform a wide range of functions in the plant cell ranging from providing energy and metabolic intermediates, via coenzyme biosynthesis and their own biogenesis to retrograde signaling and programmed cell death. To perform these functions, they contain a proteome of > 2000 different proteins expressed in some cells under some conditions. The vast majority of these proteins are imported, in many cases by a dedicated protein import machinery. Recent proteomic studies have identified about 1000 different proteins in both Arabidopsis and potato mitochondria, but even for energy-related proteins, the most well-studied functional protein group in mitochondria, < 75% of the proteins are recognized as mitochondrial by even one of six of the most widely used prediction algorithms. The mitochondrial proteomes contain proteins representing a wide range of different functions. Some protein groups, like energy-related proteins, membrane transporters, and de novo fatty acid synthesis, appear to be well covered by the proteome, while others like RNA metabolism appear to be poorly covered possibly because of low abundance. The proteomic studies have improved our understanding of basic mitochondrial functions, have led to the discovery of new mitochondrial metabolic pathways and are helping us towards appreciating the dynamic role of the mitochondria in the responses of the plant cell to biotic and abiotic stress.
- Organisation(s)
-
Institute of Plant Genetics
- External Organisation(s)
-
Yenepoya Medical College
Universidade Estadual de Campinas
University of Missouri
Aarhus University
- Type
- Article
- Journal
- MITOCHONDRION
- Volume
- 33
- Pages
- 22-37
- No. of pages
- 16
- ISSN
- 1567-7249
- Publication date
- 01.03.2017
- Publication status
- Published
- Peer reviewed
- Yes
- ASJC Scopus subject areas
- Molecular Medicine, Molecular Biology, Cell Biology
- Electronic version(s)
-
https://doi.org/10.1016/j.mito.2016.07.002 (Access:
Closed)
