The general protein-export pathway is directly required for extracellular pullulanase secretion in Escherichia coli k12
Author:
Publisher
Wiley
Subject
Molecular Biology,Microbiology
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1365-2958.1991.tb02115.x/fullpdf
Reference36 articles.
1. SecA interacts with secretory proteins by recognizing the positive charge at the amino terminus of the signal peptide in Escherichia coli.
2. Mutations which alter the function of the signal sequence of the maltose binding protein of Escherichia coli
3. PrlA is important for the translocation of exported proteins across the cytoplasmic membrane of Escherichia coli.
4. PrlA (SecY) and PrlG (SecE) interact directly and function sequentially during protein translocation in E. coli
5. The purified E. coli integral membrane protein SecYE is sufficient for reconstitution of SecA-dependent precursor protein translocation
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