SecA mediated protein translocation in Escherichia coli

The movement of proteins across or integration of proteins into the cytoplasmic membrane of Escherichia coli is mediated by the multimeric membrane protein complex translocase. The core of the translocase consists of a motor protein, the ATPase SecA, and a protein-conducting channel, formed by the integral membrane proteins SecY and SecE. The SecYE complex is highly conserved, with homologs in the cytoplasmic membrane of Archae, the chloroplast thylakoid membrane, and the eukaryotic endoplasmatic reticulum (ER). SecA is unique for the bacterial post-translational translocation pathway. It is absent both in Archaea and in the eukaryotic ER, but a homolog exists in plant chloroplasts. SecA is an soluble protein that distributes between cytoplasmic and membrane associated states. The interaction with the cytoplasmic membrane occurs via low affinity interactions with anionic phospholipids and by a high affinity interaction with the SecYEG complex. At the membrane SecA forms a receptor for preproteins and drives their stepwise movement through the SecYEG channel [93, 173]. ...

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