title: Efficient mitochondrial targeting relies on co-operation of multiple protein signals in plants.
abstract: 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.
authors.affiliation: Department of Biology, 112 Science Place, University of Saskatchewan, Saskatoon, Saskatchewan S7N 5E2, Canada.
authors.forename: Laurent
authors.initials: L
authors.lastname: Chatre
authors.forename: Loren A
authors.initials: LA
authors.lastname: Matheson
authors.forename: Andrew S
authors.initials: AS
authors.lastname: Jack
authors.forename: Sally L
authors.initials: SL
authors.lastname: Hanton
authors.forename: Federica
authors.initials: F
authors.lastname: Brandizzi
mesh_terms: D000595:Amino Acid Sequence; D004721:Endoplasmic Reticulum / Q000378:metabolism; D006056:Golgi Apparatus / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism*; D008969:Molecular Sequence Data; D050505:Mutant Proteins / Q000378:metabolism; D009154:Mutation / Q000235:genetics; D010940:Plant Proteins / Q000737:chemistry / Q000378:metabolism*; D021381:Protein Transport; D015398:Signal Transduction; D014026:Nicotiana / Q000166:cytology / Q000378:metabolism*; D014364:Tryptophan / Q000378:metabolism
chemical_list: D050505:Mutant Proteins; D010940:Plant Proteins; D014364:Tryptophan