TY - JOUR
T1 - The Enzymology of Protein Translocation across the Escherichia coli Plasma Membrane
AU - Wickner, William
AU - Driessen, Arnold J.M.
AU - Hartl, Franz-Ulrich
N1 - Relation: http://www.rug.nl/gbb/
date_submitted:2007
Rights: University of Groningen, Groningen Biomolecular Sciences and Biotechnology Institute
PY - 1991
Y1 - 1991
N2 - Converging physiological, genetic, and biochemical studies have established the salient features of preprotein translocation across the plasma membrane of Escherichia coli. Translocation is catalyzed by two proteins, a soluble chaperone and a membrane-bound translocase. SecB, the major chaperone for export, forms a complex with preproteins. Complex formation inhibits side-reactions such as aggregation and misfolding and aids preprotein binding to the membrane surface. Translocase consists of functionally linked peripheral and integral membrane protein domains. SecA protein, the peripheral membrane domain of translocase, is the primary receptor for the SecB/preprotein complex. SecA hydrolyzes ATP, promoting cycles of translocation, preprotein release, Δµ~H+-dependent translocation, and rebinding of the preprotein. The membrane-embedded domain of translocase is the SecY/E protein. It has, as subunits, the SeeY and SecE polypeptides. The SecY/E protein stabilizes and activates SecA and participates in binding it to the membrane. SecA recognizes the leader domain of preproteins, whereas both SecA and SecB recognize the mature domain. Many proteins translocate without requiring SecB, and some proteins do not need translocase to assemble into the plasma membrane. Translocation is usually followed by endoproteolytic cleavage by leader peptidase. The availability of virtually every pure protein and cloned gene involved in the translocation process makes E. coli the premier organism for the study of translocation mechanisms.
AB - Converging physiological, genetic, and biochemical studies have established the salient features of preprotein translocation across the plasma membrane of Escherichia coli. Translocation is catalyzed by two proteins, a soluble chaperone and a membrane-bound translocase. SecB, the major chaperone for export, forms a complex with preproteins. Complex formation inhibits side-reactions such as aggregation and misfolding and aids preprotein binding to the membrane surface. Translocase consists of functionally linked peripheral and integral membrane protein domains. SecA protein, the peripheral membrane domain of translocase, is the primary receptor for the SecB/preprotein complex. SecA hydrolyzes ATP, promoting cycles of translocation, preprotein release, Δµ~H+-dependent translocation, and rebinding of the preprotein. The membrane-embedded domain of translocase is the SecY/E protein. It has, as subunits, the SeeY and SecE polypeptides. The SecY/E protein stabilizes and activates SecA and participates in binding it to the membrane. SecA recognizes the leader domain of preproteins, whereas both SecA and SecB recognize the mature domain. Many proteins translocate without requiring SecB, and some proteins do not need translocase to assemble into the plasma membrane. Translocation is usually followed by endoproteolytic cleavage by leader peptidase. The availability of virtually every pure protein and cloned gene involved in the translocation process makes E. coli the premier organism for the study of translocation mechanisms.
KW - TRANSLOCASE
KW - SECRETION
KW - TRANSLOCATION ATPASE
KW - LEADER PEPTIDE
KW - PROTONMOTIVE FORCE
KW - MALTOSE-BINDING-PROTEIN
KW - SIGNAL RECOGNITION PARTICLE
KW - PROTON MOTIVE FORCE
KW - POSITIVELY CHARGED RESIDUES
KW - AMINO-ACID RESIDUES
KW - MITOCHONDRIAL PRECURSOR PROTEINS
KW - ENDOPLASMIC-RETICULUM MEMBRANE
KW - NASCENT PERIPLASMIC PROTEINS
KW - BACTERIAL LEADER PEPTIDASE
KW - CYTOPLASMIC MEMBRANE
U2 - 10.1146/annurev.bi.60.070191.000533
DO - 10.1146/annurev.bi.60.070191.000533
M3 - Review article
SN - 0066-4154
VL - 60
SP - 101
EP - 124
JO - Annual Review of Biochemistry
JF - Annual Review of Biochemistry
IS - 1
ER -