The aqueous pore through the translocon has a diameter of 40-60 angstrom during cotranslational protein translocation at the ER membrane

Article Abstract:

Translocation intermediates were constructed with fluorescent dyes and incorporated at specific sites near the nascent preprolactin to determine the internal diameter of the functioning protein translocation pore. Analysis of the incorporation of fluorescent probes into nascent secretory proteins via modified Lys-transfer RNA indicated the presence of an translocation pore with a 40-60 angstrom diameter. Furthermore, the 40-60 angstrom translocon pore was considered as the largest protein translocation pore in a membrane that maintains a permeability barrier.

Analysis, Membrane proteins, Cells, Cell permeability

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The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation

Article Abstract:

The signal sequence which plays a major role in the early stages of the translocation process of a nascent secretory protein across the endoplasmic reticulum (ER) membrane is located at an aqueous space or compartment formed by the tight binding of the ribosome to the ER membrane. The signal sequence and the nascent protein chain pass through a tunnel to reach the ER membrane. The iodide ions are prevented from entering the nascent chain pathway due to the permeability barrier between cytoplasm and the ER.

Signal peptides

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The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process

Article Abstract:

The transmembrane (TM) sequence is suggested to pass through three succesive layers in the endoplasmic reticulum (ER) membrane. The cotranslational integration of nascient proteins into the ER starts in the Sec61 alpha layer. The TM then diffuses through two translocating chain-associated membrane protein (TRAM) sites before passing diffusing into the phospholipid bi-layer. The ribosome and the transcolon are both involved in cotranslational integration.

Protein synthesis, Protein biosynthesis, Lipid membranes, Bilayer lipid membranes

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