The majority of the mitochondrial proteome, required to fulfil its diverse range of functions, is cytosolically synthesised and translocated via specialised machinery. The dedicated translocases, receptors, and associated proteins have been characterised in great detail in yeast over the last several decades, yet many of the mechanisms that regulate these processes in higher eukaryotes are still unknown. In this review, we highlight the current knowledge of mitochondrial protein import in plants. Despite the fact that the mechanisms of mitochondrial protein import have remained conserved across species, many unique features have arisen in plants to encompass the developmental, tissue-specific, and stress-responsive regulation in planta. An understanding of unique features and mechanisms in plants provides us with a unique insight into the regulation of mitochondrial biogenesis in higher eukaryotes.
Illustration of the role of glutathione in the inhibition of sickle hemoglobin polymerization: Two hemoglobin tetramers are shown in the surface representation and helical cartoon, wherein α and β globin chains are coloured magenta and cyan, respectively. The proximity of covalently bound glutathione to βCys93, represented as stick model, to the residues of the groove region is shown in yellow in the inset. βVal6 of the adjacent tetramer, the key residue in the polymerisation, is shown in spacefill model; For details, see pages 2153–2166. Image kindly provided by Amit Kumar Mandal.
Plant mitochondrial protein import: the ins and outs
Abi S. Ghifari, Mabel Gill-Hille, Monika W. Murcha; Plant mitochondrial protein import: the ins and outs. Biochem J 16 July 2018; 475 (13): 2191–2208. doi: https://doi.org/10.1042/BCJ20170521
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