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© Research
Publication : Journal of experimental botany

Efficient mitochondrial targeting relies on co-operation of multiple protein signals in plants

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Journal of experimental botany - 26 Dec 2008

Chatre L, Matheson LA, Jack AS, Hanton SL, Brandizzi F

Link to Pubmed [PMID] – 19112171

J. Exp. Bot. 2009;60(3):741-9

To date, the most prevalent model for transport of pre-proteins to plant mitochondria is based on the activity of an N-terminal extension serving as a targeting peptide. Whether the efficient delivery of proteins to mitochondria is based exclusively on the action of the N-terminal extension or also on that of other protein determinants has yet to be defined. A novel mechanism is reported here for the targeting of a plant protein, named MITS1, to mitochondria. It was found that MITS1 contains an N-terminal extension that is responsible for mitochondrial targeting. Functional dissection of this extension shows the existence of a cryptic signal for protein targeting to the secretory pathway. The first 11 amino acids of the N-terminal extension are necessary to overcome the activity of this signal sequence and target the protein to the mitochondria. These data suggest that co-operation of multiple determinants within the N-terminal extension of mitochondrial proteins may be necessary for efficient mitochondrial targeting. It was also established that the presence of a tryptophan residue toward the C-terminus of the protein is crucial for mitochondrial targeting, as mutation of this residue results in a redistribution of MITS1 to the endoplasmic reticulum and Golgi apparatus. These data suggest a novel targeting model whereby protein traffic to plant mitochondria is influenced by domains in the full-length protein as well as the N-terminal extension.

http://www.ncbi.nlm.nih.gov/pubmed/19112171