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Proteins targeted to the outer membrane also contain internal targeting signals, not all of which have been identified, and include proteins that take on a β-barrel structure, [7] such as Tom40. Some proteins however, that are targeted to the outer mitochondrial membrane contain a hydrophobic tail domain that anchors the protein to the ...
[20] [21] Protein sorting into the mitochondrial compartments always starts at the TOM complex. The TOM complex forms two exit sites for precursor proteins—Tom40, Tom7, and the intermembrane space domain of Tom22—promote the transfer of presequence-containing precursors to the TIM23 complex. [20]
The carrier preprotein is then inserted into the inner mitochondrial membrane in a potential-dependent fashion. [10] The membrane potential is necessary for both insertion of the precursor into the carrier translocase and lateral release of the protein into the lipid phase of the inner mitochondrial membrane, which completes protein translocation.
The encoded protein (PHC) catalyzes the transport of phosphate from the cytosol into the mitochondrial matrix, either by proton cotransport or in exchange for hydroxyl ions. [6] In the final steps of oxidative phosphorylation, this protein catalyzes the uptake of a phosphate ion with a proton across the mitochondrial inner membrane. [9]
The Mitochondrial-processing peptidase subunit beta precursor protein is 54.4 KDa in size and composed of 489 amino acids. The precursor protein contains a 45 amino acid N-terminal fragment as mitochondrion targeting sequence. After cleavage, the matured PMPCB protein is 49.5 KDa in size and has a theoretical pI of 5.76.
[11] [10] Precursor proteins will be transported to one of four areas of the mitochondria, which include the outer membrane, inner membrane, intermembrane space, and matrix. [ 10 ] [ 11 ] All proteins will enter the mitochondria by a translocase on the outer mitochondrial membrane (TOM).
AIFM1 is expressed as a 613-residue precursor protein that containing a mitochondrial targeting sequence (MTS) at its N-terminal and two nuclear leading sequences (NLS).). Once imported into the mitochondria, the first 54 residues of the N-terminal are cleaved to produce the mature protein, which inserts into the inner mitochondrial mem
Tim9 and Tim10 make up the group of essential small Tim proteins that assist in transport of hydrophobic precursors across the intermembrane space in mammalian cells. Both Tim9 and Tim10 form a hexamer, the Tim9-Tim10 complex, that when associated, functions as a chaperone to assist translocation of preproteins from the outer mitochondrial membrane to the translocase of the inner membrane.