Lon and Clp family proteases and chaperones share homologous substrate-recognition domains

Proceedings of the National Academy of Sciences of the United States of America

Volumn 96, Issue 12, 1999, Pages 6678-6682

  Smith, Catherine K ^a   Baker, Tania A ^a,b   Sauer, Robert T ^c  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^b HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^c NONE

Author keywords

Disassembly chaperone; Energy dependent proteases; Molecular recognition; Protein degradation; Sensor and substrate discrimination domains

Indexed keywords

CHAPERONE; PROTEINASE;

AMINO ACID SEQUENCE; ARTICLE; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; MOLECULAR INTERACTION; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN;

ADENOSINE TRIPHOSPHATASES; ATP-DEPENDENT PROTEASES; BACTERIAL PROTEINS; BINDING SITES; ENDOPEPTIDASE CLP; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HEAT-SHOCK PROTEINS; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; PROTEASE LA; PROTEIN FOLDING; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY, AMINO ACID; SERINE ENDOPEPTIDASES; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0033535955     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.96.12.6678     Document Type: Article

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