DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli.
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References (54)
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Heat-shock proteins DnaK and GroEL facilitate export of LacZ hybrid proteins in E. coli
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Escherichia coli SecB protein associates with exported protein precursors in vivo.
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ProOmpA contains secondary and tertiary structure prior to translocation and is shielded from aggregation by association with SecB protein.
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The mature portion of Escherichia coli maltose-binding protein (MBP) determines the dependence of MBP on SecB for export
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Heat-shock proteins can substitute for SecB function during protein export in Escherichia coli.
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Partial loss of function mutations in DnaK, the Escherichia coli homologue of the 70-kDa heat shock proteins, affect highly conserved amino acids implicated in ATP binding and hydrolysis.
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The folding properties of the Escherichia coli maltose-binding protein influence its interaction with SecB in vitro
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SecB-independent export of Escherichia coli ribose-binding protein (RBP): some comparisons with export of maltose-binding protein (MBP) and studies with RBP-MBP hybrid proteins
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