Phospholipid-induced monomerization and signal-peptide-induced oligomerization of SecA.

@article{Benach2003PhospholipidinducedMA,
  title={Phospholipid-induced monomerization and signal-peptide-induced oligomerization of SecA.},
  author={Jordi Obach Benach and Yi-Te Chou and John J. Fak and Anna Itkin and Daita D Nicolae and Paul J. Smith and Guenther Wittrock and Daniel L. Floyd and Cyrus M Golsaz and Lila M. Gierasch and John. F. Hunt},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 6},
  pages={
          3628-38
        }
}
The SecA ATPase drives the processive translocation of the N terminus of secreted proteins through the cytoplasmic membrane in eubacteria via cycles of binding and release from the SecYEG translocon coupled to ATP turnover. SecA forms a physiological dimer with a dissociation constant that has previously been shown to vary with temperature and ionic strength. We now present data showing that the oligomeric state of SecA in solution is altered by ligands that it interacts with during protein… CONTINUE READING
BETA

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