PMID:11563962
| Citation |
Kononova, SV, Khokhlova, OV, Zolov, SN and Nesmeyanova, MA (2001) Effect of export-specific cytoplasmic chaperone, protein SecB, on secretion of Escherichia coli alkaline phosphatase. Biochemistry Mosc. 66:803-7 |
|---|---|
| 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 degrees 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. |
| Links | |
| Keywords |
Adenosine Triphosphatases/metabolism; Alkaline Phosphatase/drug effects; Alkaline Phosphatase/secretion; Amino Acid Sequence; Bacterial Proteins/metabolism; Cytoplasm/metabolism; Escherichia coli; Escherichia coli Proteins; Membrane Transport Proteins/metabolism; Molecular Chaperones/metabolism; Molecular Chaperones/pharmacology; Protein Structure, Tertiary; Protein Transport |
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