BIOL 1090 Lecture Notes - Lecture 5: Cell Membrane, Lysosome, Lipid Bilayer

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All protein translaion begins on free ribosomes. Translaion is completed in 1 of 2 ways: translaion completed on free ribosomes. These proteins can be targeted to nucleus, mitochondria, peroxisomes, chloroplasts: translaion completed by ribosomes atached to er membrane(rough er) Ribosomes are targeted to the er membrane by a signal sequence(ss) in the protein being translated: protein contains signal sequence. Protein moves moves through channel into er=co-translaional import. Translocon: groups of 2-4; hour glass-shaped protein-lined channel in rer membrane, ring of 6 hydrophobic amino acids at centre of pore/channel, pore can be plugged by a short helical plug. A signal recogniion paricle(srp) binds to signal sequence-translaion stops. Targeing of translaion complex to er: translaion complex=[sr/ribosome/nascent polypepide, srp binds to srp receptor. Srp and srp receptors are g proteins; hydrolyze gtp. Srp is released and ribosome binds translocon; nascent polypepide passes into er lumen; signal pepide cleaved by signal peptodase; protein gets folded using er.

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