Well, let's think that I have a protein that will be transfered into ER and its signal peptide is on N terminus of the protein. I want to cleave the sequence and add it on the C-terminus. Where does my protein end up? Does the signal get to read properly?
Hello, Elif.
Theoretically, the intact peptide with signal sequence ends up into cytoplasmic protein pool after translation without being recognized by SRP because the ribosome do not expose about size of 50 amino acids sequence synthesized due to its huge size (link to Fig). The ~20 signal peptide sequence at C-terminus of the imaginary nascent peptide being synthesized is just masked by the size of ribosome.
That is a theoretical principle! However, biology has to demonstrate experimental evidences to persuade people.
http://slideplayer.com/slide/4186343/14/images/46/A+signal+sequence+of+approximately+20+amino+acids+and+rich+with+hydrophobic+amino+acids+is+often+located+at+the+N-terminus..jpg
Best wishes.
Thank you so much for your answer. I also thought of the same thing but wasn't sure. Thanks to the figure and your explanation, I fully grasped the situation.
Best regards.
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