Conditional proteolysis of the membrane protein YfgM by the FtsH protease depends on a novel N-terminal degron

Journal of Biological Chemistry

Volumn 290, Issue 31, 2015, Pages 19367-19378

  Bittner, Lisa Marie ^a   Westphal, Kai ^a   Narberhaus, Franz ^a  

^a RUHR UNIVERSITY BOCHUM   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; ESCHERICHIA COLI;

FTSH PROTEASE; GROWTH PHASE; MEMBRANE PROTEINS; N-TERMINALS; NEGATIVE REGULATORS; REGULATORY CONTROL; RESPONSE REGULATORS; STRESS CONDITION;

PROTEINS;

CYTOPLASM PROTEIN; DEGRON PROTEIN; MEMBRANE PROTEIN; PROTEIN FTSH; PROTEIN PPID; PROTEIN RCSB; PROTEIN YFGM; PROTEINASE; REGULATOR PROTEIN; UNCLASSIFIED DRUG; ADENOSINE TRIPHOSPHATE DEPENDENT PROTEINASE; CHAPERONE; ESCHERICHIA COLI PROTEIN; FTSH PROTEIN, E COLI; PEPTIDYLPROLYL ISOMERASE; PPID PROTEIN, E COLI; RCSB PROTEIN, E COLI; TRANSCRIPTION FACTOR; YFGM PROTEIN, E COLI;

AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIAL GENE; CELL PROTECTION; CONTROLLED STUDY; ESCHERICHIA COLI; GENE EXPRESSION REGULATION; GENE OVEREXPRESSION; GENETIC VARIABILITY; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DETERMINATION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; YFGM GENE; AMINO ACID SEQUENCE; CHEMISTRY; METABOLISM; MOLECULAR GENETICS; PHYSIOLOGICAL STRESS; PHYSIOLOGY; PROTEIN STABILITY;

AMINO ACID SEQUENCE; ATP-DEPENDENT PROTEASES; ESCHERICHIA COLI PROTEINS; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; PEPTIDYLPROLYL ISOMERASE; PROTEIN STABILITY; PROTEOLYSIS; STRESS, PHYSIOLOGICAL; TRANSCRIPTION FACTORS;

EID: 84940482735     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.648550     Document Type: Article

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