TY  - JOUR
A1  - Keyzer, Jeanine de
A1  - Sluis, Eli O. van der
A1  - Spelbrink, Robin E. J.
A1  - Nijstad, Niels
A1  - Kruijff, Ben de
A1  - Nouwen, Nico
A1  - Does, Chris van der
A1  - Driessen, Arnold J. M.
T1  - Covalently dimerized SecA is functional in protein translocation
T2  - Journal of biological chemistry
N2  - The ATPase SecA provides the driving force for the transport of secretory proteins across the cytoplasmic membrane of Escherichia coli. SecA exists as a dimer in solution, but the exact oligomeric state of SecA during membrane binding and preprotein translocation is a topic of debate. To study the requirements of oligomeric changes in SecA during protein translocation, a non-dissociable SecA dimer was formed by oxidation of the carboxyl-terminal cysteines. The cross-linked SecA dimer interacts with the SecYEG complex with a similar stoichiometry as non-cross-linked SecA. Cross-linking reversibly disrupts the SecB binding site on SecA. However, in the absence of SecB, the activity of the disulfide-bonded SecA dimer is indistinguishable from wild-type SecA. Moreover, SecYEG binding stabilizes a cold sodium dodecylsulfate-resistant dimeric state of SecA. The results demonstrate that dissociation of the SecA dimer is not an essential feature of the protein translocation reaction.
Y1  - 2021
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/76207
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-762078
SN  - 0021-9258
VL  - 280.2005
IS  - 42
SP  - 35255
EP  - 35260
PB  - American Society for Biochemistry and Molecular Biology Publications
CY  - Bethesda, Md
ER  -