Activity of the mycobacterial proteasomal ATPase Mpa is reversibly regulated by pupylation

Journal of Biological Chemistry

Volumn 287, Issue 11, 2012, Pages 7907-7914

  Delley, Cyrille L ^a   Striebel, Frank ^a,b   Heydenreich, Franziska M ^a   Özcelik, Dennis ^a   Weber Ban, Eilika ^a  

^a ETH ZURICH   (Switzerland)

^b MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

C-TERMINAL REGIONS; CORE PARTICLES; ENZYMATIC ACTIVITIES; LYSINE RESIDUES; MYCOBACTERIAL; MYCOBACTERIUM TUBERCULOSIS; POST-TRANSLATIONAL MODIFICATIONS; PROTEASOMAL DEGRADATION; PROTEASOMES; TARGET PROTEINS; UBIQUITIN-LIKE PROTEINS;

DEGRADATION;

AMINO ACIDS;

BACTERIAL ENZYME; DOP PROTEIN; LIGASE; LYSINE; MPA PROTEIN; PAFA PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DEPUPYLATION; ENZYME ACTIVITY; ENZYME BINDING; ENZYME INACTIVATION; ENZYME REGULATION; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN MODIFICATION; PROTEIN PROCESSING; PUPYLATION;

ADENOSINE TRIPHOSPHATASES; AMIDOHYDROLASES; BACTERIAL PROTEINS; MYCOBACTERIUM TUBERCULOSIS; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN FOLDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEOLYSIS; UBIQUITINS; VIRULENCE FACTORS;

BACTERIA (MICROORGANISMS); MYCOBACTERIUM TUBERCULOSIS; PROKARYOTA;

EID: 84858039698     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.331124     Document Type: Article

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