The bacterial ATPase SecA functions as a monomer in protein translocation - PubMed (original) (raw)

. 2005 Mar 11;280(10):9097-105.

doi: 10.1074/jbc.M413947200. Epub 2004 Dec 23.

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• PMID: 15618215
• DOI: 10.1074/jbc.M413947200

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The bacterial ATPase SecA functions as a monomer in protein translocation

Eran Or et al. J Biol Chem. 2005.

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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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