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  • Title: The bacterial ATPase SecA functions as a monomer in protein translocation.
    Author: Or E, Boyd D, Gon S, Beckwith J, Rapoport T.
    Journal: J Biol Chem; 2005 Mar 11; 280(10):9097-105. PubMed ID: 15618215.
    Abstract:
    The ATPase SecA drives the post-translational translocation of proteins through the SecY channel in the bacterial inner membrane. SecA is a dimer that can dissociate into monomers under certain conditions. To address the functional importance of the monomeric state, we generated an Escherichia coli SecA mutant that is almost completely monomeric (>99%), consistent with predictions from the crystal structure of Bacillus subtilis SecA. In vitro, the monomeric derivative retained significant activity in various assays, and in vivo, it sustained 85% of the growth rate of wild type cells and reduced the accumulation of precursor proteins in the cytoplasm. Disulfide cross-linking in intact cells showed that mutant SecA is monomeric and that even its parental dimeric form is dissociated. Our results suggest that SecA functions as a monomer during protein translocation in vivo.
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