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Characterization of the supporting role of SecE in protein translocation
Author(s) -
Lycklama a Nijeholt Jelger A.,
de Keyzer Jeanine,
Prabudiansyah Irfan,
Driessen Arnold J.M.
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.07.046
Subject(s) - transmembrane protein , chromosomal translocation , translocase , translocon , chemistry , cleavage (geology) , n terminus , transmembrane domain , transport protein , biophysics , biochemistry , microbiology and biotechnology , peptide sequence , biology , amino acid , gene , paleontology , receptor , fracture (geology)
SecYEG functions as a membrane channel for protein export. SecY constitutes the protein‐conducting pore, which is enwrapped by SecE in a V‐shaped manner. In its minimal form SecE consists of a single transmembrane segment that is connected to a surface‐exposed amphipathic α‐helix via a flexible hinge. These two domains are the major sites of interaction between SecE and SecY. Specific cleavage of SecE at the hinge region, which destroys the interaction between the two SecE domains, reduced translocation. When SecE and SecY were disulfide bonded at the two sites of interaction, protein translocation was not affected. This suggests that the SecY and SecE interactions are static, while the hinge region provides flexibility to allow the SecY pore to open.