Requirement for the COOH-terminal pro-sequence in the translocation of aqualysin I across the cytoplasmic membrane in Escherichia coli

Biochemical and Biophysical Research Communications

Volumn 277, Issue 1, 2000, Pages 216-220

  Kim, Dong Wook ^a   Matsuzawa, Hiroshi ^a  

^a UNIVERSITY OF TOKYO   (Japan)

Author keywords

Aqualysin I; C terminal pro sequence; Intramolecular chaperone; Protein secretion; Protein translocation; Serine protease

Indexed keywords

QUALYSIS I; SIGNAL PEPTIDE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL MEMBRANE; CHROMOSOME TRANSLOCATION; ENZYME SYNTHESIS; ESCHERICHIA COLI; EXTRACELLULAR SPACE; GENE DELETION; GENE MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN SECRETION; SIGNAL TRANSDUCTION; THERMUS AQUATICUS;

ANIMALIA; ESCHERICHIA COLI; NEGIBACTERIA; THERMUS AQUATICUS;

EID: 0034649196     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.2000.3657     Document Type: Article

References (20)

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3. Role of the COOH-terminal pro-sequence of aqualysin I (a heat-stable serine protease) in its extracellular secretion by Thermus thermophilus
4. Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease
5. Involvement of the COOH-terminal pro-sequence of Serratia marcescens serine protease in the folding of the mature enzyme
6. Production of thermophilic extracellular proteases (aqualysins I and II) by Thermus aquaticus YT-1, an extreme thermophile
7. Purification and characterization of aqualysin I (a thermophilic alkaline serine protease) produced by Thermus aquaticus YT-1
8. Nucleotide sequence of the gene for aqualysin I (a thermophilic alkaline serine protease) of Thermus aquaticus YT-1 and characteristics of the deduced primary structure of the enzyme
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13. Cleavage of structural proteins during the assembly of the head of bacteriophage T4
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17. Successive action of Escherichia coli chaperones in vivo
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