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The translocon (also known as a translocator or translocation channel) is a complex of proteins associated with the translocation of polypeptides across membranes. [1] In eukaryotes the term translocon most commonly refers to the complex that transports nascent polypeptides with a targeting signal sequence into the interior (cisternal or lumenal) space of the endoplasmic reticulum (ER) from ...
A diagram of a chloroplast. The TIC and TOC complexes are located on different sides of the chloroplast membrane.. The TIC and TOC complexes are translocons located in the chloroplast of a eukaryotic cell, that is, protein complexes that facilitate the transfer of proteins in and out through the chloroplast's membrane.
The SecY protein is the main transmembrane subunit of the bacterial Sec export pathway and of a protein-secreting ATPase complex, also known as a SecYEG translocon.Homologs of the SecYEG complex are found in eukaryotes and in archaea, where the subunit is known as Sec61α.
Eukaryotic translocon uses BiP. The structure of human Sec61 is resolved at 3.84 Å by cryo-EM in 2020, together with the rest of the co-translational translocon including the ribosome. [5] The archaeal translocon is less understood. It might use SecDF-YajC and YidC like bacteria, as homologs have been found. An ATPase is yet to be identified. [6]
SRP then targets this entire complex (the ribosome-nascent chain complex) to the protein-conducting channel, also known as the translocon, in the endoplasmic reticulum (ER) membrane. This occurs via the interaction and docking of SRP with its cognate SRP receptor [6] that is located in close proximity to the translocon.
23480 20335 Ensembl ENSG00000132432 ENSMUSG00000078974 UniProt P60059 P60060 RefSeq (mRNA) NM_014302 NM_001012456 NM_001109971 NM_001109972 NM_011343 RefSeq (protein) NP_001012474 NP_055117 NP_001103441 NP_001103442 NP_035473 Location (UCSC) Chr 7: 54.75 – 54.76 Mb Chr 11: 16.5 – 16.51 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Protein transport protein Sec61 subunit gamma ...
The translocase of the outer membrane (TOM) forms a complex made of Tom70, Tom22, and Tom20, along with Tom40, Tom7, Tom6, and Tom5.Tom20 and Tom22 are preprotein receptors, which are responsible for recognition of the cleavable presequence possessed by mitochondrial-targeted proteins. [9]
The translocon channel provides a highly heterogeneous environment for the nascent transmembrane α-helices. A relatively polar amphiphilic α-helix can adopt a transmembrane orientation in the translocon (although it would be at the membrane surface or unfolded in vitro ), because its polar residues can face the central water-filled channel of ...