Effect of export-specific cytoplasmic chaperone, protein SecB, on secretion of Escherichia coli alkaline phosphatase.
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.
Kononova
S V
SV
Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia.
Khokhlova
O V
OV
Zolov
S N
SN
Nesmeyanova
M A
MA
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000469:Alkaline Phosphatase / Q000187:drug effects / Q000378:metabolism*; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000378:metabolism*; D003593:Cytoplasm / Q000378:metabolism; D004926:Escherichia coli; D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins / Q000378:metabolism*; D018832:Molecular Chaperones / Q000378:metabolism* / Q000494:pharmacology; D017434:Protein Structure, Tertiary; D021381:Protein Transport; D000069816:SEC Translocation Channels; D000081416:SecA Proteins
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins; D018832:Molecular Chaperones; D000069816:SEC Translocation Channels; D000469:Alkaline Phosphatase; D000251:Adenosine Triphosphatases; D000081416:SecA Proteins