The process of directing proteins towards and into the mitochondrion, usually mediated by mitochondrial proteins that recognize signals contained within the imported protein.
Organism
Arabidopsis thaliana
Click Gene ID to show a list of co-expressed genes.
ATTOC64-V (ARABIDOPSIS THALIANA TRANSLOCON AT THE OUTER MEMBRANE OF CHLOROPLASTS 64-V)
F:amidase activity, binding, carbon-nitrogen ligase activity, with glutamine as amido-N-donor;P:protein targeting to mitochondrion;C:mitochondrion;BOMFPA
One of two loci encoding the TIM44 subunit of the mitochondrial inner membrane translocase complex. TIM44 subunit is the part of the complex that hydrolyzes ATP to provide energy for protein translocation to the inner membrane.
One of two genes in Arabidopsis that encode a putative subunit of the mitochondrial inner membrane translocase complex. TIM44 subunit is thought to provide the energy for translocation via hydrolysis of ATP.
Subunit of the TOM complex, a translocase in the outer mitochondrial membrane that selectively allows proteins with a mitochondrial targeting sequence to enter the mitochondrion.
Encodes a component of the TOM receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. With TOM22, functions as the transit peptide receptor at the surface of the mitochondrial outer membrane and facilitates the movement of preproteins into the translocation pore.
Subunit of the TOM complex, a translocase in the outer mitochondrial membrane that selectively allows proteins with a mitochondrial targeting sequence to enter the mitochondrion.
The process of targeting specific proteins to particular membrane-bounded subcellular organelles. Usually requires an organelle specific protein sequence motif.
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a mitochondrion; includes mitochondrial morphogenesis and distribution, and replication of the mitochondrial genome as well as synthesis of new mitochondrial components.
The cleavage of proteins, usually near the N terminus, during the process of import into the mitochondrion; several different peptidases mediate cleavage of proteins destined for different mitochondrial compartments.
The import of proteins across the outer and inner mitochondrial membranes into the matrix. Unfolded proteins enter the mitochondrial matrix with a chaperone protein; the information required to target the precursor protein from the cytosol to the mitochondrial matrix is contained within its N-terminal matrix-targeting sequence. Translocation of precursors to the matrix occurs at the rare sites where the outer and inner membranes are close together.
The import of proteins into the mitochondria inner membrane. Inner membrane proteins are first imported into the matrix space where the matrix-targeting sequence is removed; how these proteins then are incorporated into the inner membrane is not known.
The import of proteins into the outer membrane of the mitochondrion. Outer membrane proteins have a short matrix-targeting sequence followed by a long stretch of hydrophobic amino acids at the N-terminus. The hydrophobic sequence functions as a stop-transfer sequence that both prevents transfer of the protein into the matrix and anchors it as an integral protein in the outer membrane.
