SecA alone can promote protein translocation and ion channel activity: SecYEG increases efficiency and signal peptide specificity.

@article{Hsieh2011SecAAC,
  title={SecA alone can promote protein translocation and ion channel activity: SecYEG increases efficiency and signal peptide specificity.},
  author={Ying-hsin Hsieh and Hao Zhang and Bor-ruei Lin and Ningren Cui and Bing Na and Hsiuchin Yang and Chun Jiang and Sen-fang Sui and Phang C. Tai},
  journal={The Journal of biological chemistry},
  year={2011},
  volume={286 52},
  pages={44702-9}
}
SecA is an essential component of the Sec-dependent protein translocation pathway across cytoplasmic membranes in bacteria. Escherichia coli SecA binds to cytoplasmic membranes at SecYEG high affinity sites and at phospholipid low affinity sites. It has been widely viewed that SecYEG functions as the essential protein-conducting channel through which precursors cross the membranes in bacterial Sec-dependent pathways, and that SecA functions as a motor to hydrolyze ATP in translocating… CONTINUE READING

Connections & Topics

Mentioned Connections BETA
The results show that SecA alone is sufficient to promote protein translocation into liposomes and to elicit ionic channel activity at the phospholipids low affinity binding sites , thus indicating that SecA is able to form the protein - conducting channels .
The results show that SecA alone is sufficient to promote protein translocation into liposomes and to elicit ionic channel activity at the phospholipids low affinity binding sites , thus indicating that SecA is able to form the protein - conducting channels .
All Topics