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What happens if all the signal peptides in a cell are destroyed?
Would the ribosome be degraded? Would all the proteins end up in the cytoplasm? Would they get stuck in the ER? Would vesicles be able to form?
My guess is that they would end up in the cytoplasm. The only thing I'm concerned about is the hydrophobic to hydrophobic interaction.
If you remove the signal peptide from the genes of exported proteins, then they will end up staying in the cytoplasm. The ribosomes translating them will not be moved onto the ER membrane because there is no signal sequence for SRP to recognize.
|cell , destroyed , peptides , signal|
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