Two distinct ATP-binding domains are needed to promote protein export by Escherichia coli SecA ATPase
Author:
Publisher
Wiley
Subject
Molecular Biology,Microbiology
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1365-2958.1993.tb00921.x/fullpdf
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1. Reconstitution of a protein translocation system containing purified SecY, SecE, and SecA from Escherichia coli.
2. SecA interacts with secretory proteins by recognizing the positive charge at the amino terminus of the signal peptide in Escherichia coli.
3. SecA, an essential component of the secretory machinery of Escherichiacoli, exists as homodimer
4. Directed mutagenesis of the strongly conserved aspartate 242 in the beta-subunit of Escherichia coli proton-ATPase.
5. Regulation by ATP and ADP of CFTR Chloride Channels That Contain Mutant Nucleotide-Binding Domains
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