Abstract
The efficiency of secretion of Escherichia coli alkaline phosphatase depends on the presence in cells of a cytoplasmic chaperone—protein SecB. Secretion increases in the presence of this chaperone at 30°C, which is the most favorable for the interaction of SecB with the export-initiation domain found previously in the N-terminal region of the mature enzyme. This interaction most likely occurs in the region of the export domain, which is located close to the signal peptide and in complex with a translocational ATPase—protein SecA.
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Kononova, S.V., Khokhlova, O.V., Zolov, S.N. et al. Effect of Export-Specific Cytoplasmic Chaperone, Protein SecB, on Secretion of Escherichia coli Alkaline Phosphatase. Biochemistry (Moscow) 66, 803–807 (2001). https://doi.org/10.1023/A:1010225131673
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DOI: https://doi.org/10.1023/A:1010225131673