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Three small proteins Tom5, Tom6, Tom7 interact closely with Tom40 to assemble and stabilize the complex. The TOM complex also consists of a dimer of Tom40 or small Tom proteins that are held together by two Tom22 subunits. [20] [21] Protein sorting into the mitochondrial compartments always starts at the TOM complex. The TOM complex forms two ...
The TIM/TOM complex is a protein complex in cellular biochemistry which translocates proteins produced from nuclear DNA through the mitochondrial membrane for use in oxidative phosphorylation. In enzymology , the complex is described as an mitochondrial protein-transporting ATPase ( EC 7.4.2.3 ), or more systematically ATP phosphohydrolase ...
The translocase of the outer membrane (TOM) is a complex of proteins found in the outer mitochondrial membrane of the mitochondria. It allows movement of proteins through this barrier and into the intermembrane space of the mitochondrion. Most of the proteins needed for mitochondrial function are encoded by the nucleus of the cell.
Protein targeting or protein sorting is the biological mechanism by which proteins are transported to their appropriate destinations within or outside the cell. [ 1 ] [ 2 ] [ note 1 ] Proteins can be targeted to the inner space of an organelle , different intracellular membranes , the plasma membrane , or to the exterior of the cell via secretion .
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.
ATFS-1 has a nuclear localization sequence that allows it to be imported into the nucleus as well as an N-terminal mitochondrial targeting sequence (MTS) that allows for import into the mitochondria. [12] In healthy cells, ATFS-1 is preferentially targeted to the mitochondrial matrix where it is degraded by the Lon protease.
Many MC proteins preferentially catalyze the exchange of one solute for another ().A variety of these substrate carrier proteins, which are involved in energy transfer, have been found in the inner membranes of mitochondria and other eukaryotic organelles such as the peroxisome and facilitate the transport of inorganic ions, nucleotides, amino acids, keto acids and cofactors across the membrane.
The sorting and assembly machinery is required for the assembly of beta barrel proteins, this includes proteins such as the Tom40 import pore and porin.. Like all mitochondrial proteins, beta barrel proteins are transported into the intermembrane space of mitochondria via the translocase of the outer membrane.