Maximal efficiency of coupling between ATP hydrolysis and translocation of polypeptides mediated by secB requires two protomers of secA

Abstract

SecA is the ATPase that provides energy for translocation of precursor polypeptides through the SecYEG translocon in Escherichia coli during protein export. We have previously shown that when SecA receives the precursor from SecB the ternary complex is fully active only when two protomers of SecA are bound. Here we have used variants of SecA and of SecB that populate complexes containing two protomers of SecA to different degrees to examine both the hydrolysis of ATP and the translocation of polypeptides. We conclude that the low activity of the complexes with only one protomer is the result of a low efficiency of coupling between ATP hydrolysis and translocation.