MICR 221 Lecture Notes - Lecture 9: Pilus, Protein Precursor, Signal Peptide

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Signal peptides: most, not all, proteins to be secreted from the cell are made with n-terminal signal peptide. Signal peptidase (spi or spii) cleaves signal peptide. Can be co-translational, can start before protein is completely translated on ribosome, will be fed through while the rest is being made. Cytoplasm events: proteins to be exported are prevented from folding by chaperone secb, secb has seca binding ability so delivers bound protein to seca. Preprotein bearing seca binds to cm at high affinity seca binding site composed of secy and sece. Translocation initiation begins: signal peptide region inserts into cm, leading to cleavage site exposed on periplasmic side and 20-30 mature residues in the cm (already in the channel) Sec-dependent pathway seca bound to the channel hydrolyzing atp once the cleavage site bcomes available, cleaved off eventually whole protein goes through, ends up in periplasm.

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