The N-degradome of Escherichia coli: Limited proteolysis in vivo generates a large pool of proteins bearing N-degrons

Journal of Biological Chemistry

Volumn 288, Issue 40, 2013, Pages 28913-28924

  Humbard, Matthew A ^a   Surkov, Serhiy ^a   De Donatis, Gian Marco ^a,b   Jenkins, Lisa M ^a   Maurizi, Michael R ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

^b UNIVERSITY OF CINCINNATI   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENDOPROTEOLYTIC CLEAVAGE; IN-VIVO; LIMITED PROTEOLYSIS; NATIVE PROTEINS; POSSIBLE MECHANISMS;

ESCHERICHIA COLI;

PROTEINS;

ALANINE; ARGININE; BACTERIAL PROTEIN; LYSINE; N DEGRON CONTAINING PROTEIN; PHENYLALANINE; PROTEIN CLPS; THREONINE; UNCLASSIFIED DRUG; VALINE;

ARTICLE; BACTERIAL CELL; BACTERIAL GROWTH; BINDING AFFINITY; CELL DIVISION; CONTROLLED STUDY; DNA REPLICATION; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN MODIFICATION; PROTEIN PROCESSING; PROTEIN SYNTHESIS;

AAT; ADAPTOR PROTEINS; ATP-DEPENDENT PROTEASE; CLPA; CLPS; END SITE; N-END RULE; PROTEIN DEGRADATION; PROTEIN PROCESSING; PROTEOMICS;

AMINO ACID SEQUENCE; AMINO ACIDS; CHROMATOGRAPHY, AFFINITY; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; IMMOBILIZED PROTEINS; MASS SPECTROMETRY; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEOLYSIS; RECOMBINANT FUSION PROTEINS; SEQUENCE ANALYSIS, PROTEIN;

EID: 84885123033     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.492108     Document Type: Article

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