Processive degradation of unstructured protein by escherichia coli lon occurs via the slow, sequential delivery of multiple scissile sites followed by rapid and synchronized peptide bond cleavage events

Biochemistry

Volumn 52, Issue 33, 2013, Pages 5629-5644

  Mikita, Natalie ^a,b   Cheng, Iteen ^a,b   Fishovitz, Jennifer ^a,b   Huang, Jonathan ^a,b   Lee, Irene ^a,b  

^a CASE WESTERN RESERVE UNIVERSITY   (United States)

^b UNIVERSITY OF NOTRE DAME   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ATP-DEPENDENT PROTEASE; CARBOXYL-TERMINAL; PHYSIOLOGICAL SUBSTRATE; PROTEIN DEGRADATION; PROTEOLYTIC MECHANISMS; SEQUENTIAL DELIVERY; SPECTROMETRY TECHNIQUE; TRANSIENT KINETICS;

ESCHERICHIA COLI; KINETICS; PEPTIDES;

SUBSTRATES;

ADENOSINE TRIPHOSPHATE DEPENDENT PROTEINASE; BACTERIAL PROTEIN; ENDOPEPTIDASE LA; GUANINE NUCLEOTIDE BINDING PROTEIN;

ARTICLE; CARBOXY TERMINAL SEQUENCE; ESCHERICHIA COLI; KINETICS; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN CLEAVAGE; PROTEIN DEGRADATION;

AMINO ACID SEQUENCE; ATP-DEPENDENT PROTEASES; BINDING SITES; BLOTTING, WESTERN; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; FLUORESCENCE RESONANCE ENERGY TRANSFER; KINETICS; MASS SPECTROMETRY; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PEPTIDES; PROTEASE LA; PROTEOLYSIS; SUBSTRATE SPECIFICITY;

EID: 84882604985     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi4008319     Document Type: Article

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