Cage assembly of DegP protease is not required for substrate-dependent regulation of proteolytic activity or high-temperature cell survival

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

Volumn 109, Issue 19, 2012, Pages 7263-7268

  Kim, Seokhee ^a   Sauer, Robert T ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

Macromolecular assembly; Periplasmic degradation; Protein quality control; Stress survival

Indexed keywords

ENZYME VARIANT; OLIGOMER; PROTEINASE; PROTEINASE DEGP; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL CELL; BACTERIAL GROWTH; BACTERIAL SURVIVAL; CELL SURVIVAL; CONTROLLED STUDY; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; HIGH TEMPERATURE; MOLECULAR MODEL; NONHUMAN; PDZ DOMAIN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DEGRADATION; WILD TYPE;

BLOTTING, WESTERN; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; FLUORESCENCE POLARIZATION; FLUORESCENCE RESONANCE ENERGY TRANSFER; HEAT-SHOCK PROTEINS; KINETICS; MICROBIAL VIABILITY; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MUTATION; PERIPLASMIC PROTEINS; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, TERTIARY; PROTEOLYSIS; SERINE ENDOPEPTIDASES; SUBSTRATE SPECIFICITY; TEMPERATURE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 84860816318     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1204791109     Document Type: Article

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