A membrane-bound archaeal Lon protease displays ATP-independent proteolytic activity towards unfolded proteins and ATP-dependent activity for folded proteins

Journal of Bacteriology

Volumn 184, Issue 13, 2002, Pages 3689-3698

  Fukui, Toshiaki ^a   Eguchi, Tomohiro ^a   Atomi, Haruyuki ^a   Imanaka, Tadayuki ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ENDOPEPTIDASE LA; MEMBRANE ENZYME; PROTEINASE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CATALYSIS; ENZYME ACTIVITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; SEQUENCE HOMOLOGY; THERMOCOCCUS; THERMOSTABILITY;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; ARCHAEAL PROTEINS; ATP-DEPENDENT PROTEASES; BASE SEQUENCE; CELL MEMBRANE; CLONING, MOLECULAR; ESCHERICHIA COLI PROTEINS; HEAT-SHOCK PROTEINS; MOLECULAR SEQUENCE DATA; PROTEASE LA; PROTEIN FOLDING; RECOMBINANT PROTEINS; SERINE ENDOPEPTIDASES; SUBSTRATE SPECIFICITY; TEMPERATURE; THERMOCOCCUS;

ARCHAEA; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; EUKARYOTA; THERMOCOCCUS; THERMOCOCCUS KODAKARAENSIS;

EID: 0036283446     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.184.13.3689-3698.2002     Document Type: Article

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