SecA Dimer Cross-Linked at Its Subunit Interface Is Functional for Protein Translocation
2006 ◽
Vol 188
(1)
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pp. 335-338
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Keyword(s):
ABSTRACT SecA facilitates protein transport across the eubacterial plasma membrane by its association with cargo proteins and the SecYEG translocon, followed by ATP-driven conformational changes that promote protein translocation in a stepwise manner. Whether SecA functions as a monomer or a dimer during this process has been the subject of considerable controversy. Here we utilize cysteine-directed mutagenesis along with the crystal structure of the SecA dimer to create a cross-linked dimer at its subunit interface, which was normally active for in vitro protein translocation.
Keyword(s):
2021 ◽
Vol 118
(35)
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pp. e2101287118
2007 ◽
Vol 178
(4)
◽
pp. 611-620
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2018 ◽
2019 ◽
1989 ◽
Vol 264
(4)
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pp. 2242-2249
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