Identification of signals required for import of the soybean F(A)d subunit of ATP synthase into mitochondria.

The requirements for protein import into mitochondria was investigated by using the targeting signal of the F(A)d subunit of soybean mitochondrial ATP synthase attached to two different passenger proteins, its native passenger and soybean alternative oxidase. Both passenger proteins are soybean mitochondrial proteins. Changing hydrophobic residues at positions -24:25 (Phe:Leu), -18:19 (Ile:Leu) and -12:13 (Leu:Ile) of the 31 amino acid cleavable presequence gave more than 50% inhibition of import with both passenger proteins.

A transcriptomic and proteomic characterization of the Arabidopsis mitochondrial protein import apparatus and its response to mitochondrial dysfunction.

Mitochondria import hundreds of cytosolically synthesized proteins via the mitochondrial protein import apparatus. Expression analysis in various organs of 19 components of the Arabidopsis mitochondrial protein import apparatus encoded by 31 genes showed that although many were present in small multigene families, often only one member was prominently expressed. This was supported by comparison of real-time reverse transcriptase-polymerase chain reaction and microarray experimental data with expressed sequence tag numbers and massive parallel signature sequence data.