Lecture 5: Protein Export Flashcards
Localization Signal
Portion of the polypeptide usually in the primary sequence that acts as a signal for where the protein needs to go. Often on N-terminus
Secretion Signal
One of the localization signals whose cleavage can reduce improper folding which may negatively impact normal cell processes
-Characteristic features include partially conserved sequence of amino acids and location in nascent polypeptides
-Recognized by a specific secretion system
-May not be present in the mature protein
Most proteins in the outer membrane
Beta barrels
Most proteins in the inner membrane
Alpha helix transmembrane domain
Sec/Tat dependent secretion system
-In gram positive: Movement of protein from inner membrane to the outer membrane
-In gram negative: Into the periplasm
Type 2 secretion system
Gets protein out of the cell past the outer membrane completely
Type 5 secretion system
Gets protein INTO the outer membrane
Common characteristics of all protein secretion systems
-All involve multi protein complexes to cross on or more membranes
-Structurally unique from one another
-Each has a unique mailing label in the nascent polypeptide
-Secrete different proteins
-Have some kind of energy source to drive membrane translocation
-Many translocation systems use cytoplasmic chaperones to restrict folding of the peptide until secreted
Sec-dependent secretion systems (3 characteristics)
-Dominant protein secretion mechanism that crosses cytoplasmic/inner membrane
-Present in ALL bacteria
-Contains a N-terminal secretion signal
SecYEG/BA characteristics
-In both gram positive and negative
-Transport of unfolded proteins
SecYEG/BA Mechanism
-SecB recognizes a secretion signal and acts as a chaperone to transport and prevent unfolding towards YEG
-SecA uses ATPase activity (ATP hydrolysis) that guides the unfolded protein through SecYEG via translocation
-Secretion signal is cleaved (Usually from N-term)
SecSRP chracteristics
-Both gram positive & gram negative
-Cotranslational Transport
-Uses signal recognition particle (SRP) to for secretion signal recognition
-N-term is synthesized first by ribosome in order for it to be recognized by SecYEG
SecSRP Mechanism
-SRP binds to co-translated protein from ribosome while still attached
-FtsY uses GTPase activity to dock the ribosome-SRP complex to SecYEG
-SecYEG supports translocation INTO the membrane to become an intermembrane protein
Twin Arginine Translocation (TAT) secretion system pathway characteristics
-Found in gram positive & gram negative bacteria
-Transports (FOLDED) proteins
-Uses proton motive force as energy
TAT secretion system pathway
-TatB and TatC bind N-terminal peptide with twin arginines
-TatB and TatC recruit this peptide to TatA that acts as a membrane channel for translocation