Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway

EMBO Reports

Volumn 11, Issue 10, 2010, Pages 791-797

  Imkamp, Frank ^a   Striebel, Frank ^a   Sutter, Markus ^a   Özcelik, Dennis ^a   Zimmermann, Natalie ^a   Sander, Peter ^b   Weber Ban, Eilika ^a  

^a ETH ZURICH   (Switzerland)

^b UNIVERSITY OF ZURICH   (Switzerland)

Author keywords

depupylation; Dop; Mpa; proteasome; pupylation

Indexed keywords

ADENOSINE TRIPHOSPHATASE; AMIDASE; BACTERIAL PROTEIN; DEPUPYLASE; PROTEIN DOP; UBIQUITIN; UNCLASSIFIED DRUG;

ARTICLE; CORYNEBACTERIUM; ENZYME ACTIVITY; ENZYME SUBSTRATE; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN MODIFICATION; PROTEIN PROCESSING; SIGNAL TRANSDUCTION;

BACTERIAL PROTEINS; GLUTAMINE; LIGASES; LYSINE; MYCOBACTERIUM TUBERCULOSIS; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN PROCESSING, POST-TRANSLATIONAL; UBIQUITINS;

BACTERIA (MICROORGANISMS); EUKARYOTA; PROKARYOTA;

EID: 77957231199     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.1038/embor.2010.119     Document Type: Article

References (16)

1. Burns KE, Liu WT, Boshoff HI, Dorrestein PC, Barry CE III (2009) Proteasomal protein degradation in Mycobacteria is dependent upon a prokaryotic ubiquitin-like protein. J Biol Chem 284: 3069-3075
2. Burns KE, Pearce MJ, Darwin KH (2010) Prokaryotic ubiquitin-like protein provides a two-part degron to Mycobacterium proteasome substrates. J Bacteriol 192: 2933-2935
3. Finley D (2009) Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu Rev Biochem 78: 477-513
4. Humbard MA, Miranda HV, Lim JM, Krause DJ, Pritz JR, Zhou G, Chen S, Wells L, Maupin-Furlow JA (2010) Ubiquitin-like small archaeal modifier proteins (SAMPs) in Haloferax volcanii. Nature 463: 54-60
5. Imkamp F, Rosenberger T, Striebel F, Keller PM, Amstutz B, Sander P, Weber-Ban E (2010) Deletion of dop in Mycobacterium smegmatis abolishes pupylation of protein substrates in vivo. Mol Microbiol 75: 744-754
6. Iyer LM, Burroughs AM, Aravind L (2008) Unraveling the biochemistry and provenance of pupylation: a prokaryotic analog of ubiquitination. Biol Direct 3: 45
7. Kerscher O, Felberbaum R, Hochstrasser M (2006) Modification of proteins by ubiquitin and ubiquitin-like proteins. Annu Rev Cell Dev Biol 22: 159-180
8. Pearce MJ, Arora P, Festa RA, Butler-Wu SM, Gokhale RS, Darwin KH (2006) Identification of substrates of the Mycobacterium tuberculosis proteasome. EMBO J 25: 5423-5432 (Pubitemid 44764151)
9. Pearce MJ, Mintseris J, Ferreyra J, Gygi SP, Darwin KH (2008) Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis. Science 322: 1104-1107
10. Reyes-Turcu FE, Ventii KH, Wilkinson KD (2009) Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes. Annu Rev Biochem 78: 363-397
11. Sander P, Meier A, Böttger EC (1995) rpsL?: a dominant selectable marker for gene replacement in mycobacteria. Mol Microbiol 16: 991-1000
12. Striebel F, Imkamp F, Sutter M, Steiner M, Mamedov A, Weber-Ban E (2009) Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes. Nat Struct Mol Biol 16: 647-651
13. Striebel F, Hunkeler M, Summer H, Weber-Ban E (2010) The mycobacterial Mpa-proteasome unfolds and degrades pupylated substrates by engaging Pup0s N-terminus. EMBO J 29: 1262-1271
14. Sutter M, Damberger FF, Imkamp F, Allain FH, Weber-Ban E (2010) Prokaryotic ubiquitin-like protein (Pup) is coupled to substrates via the side chain of its C-terminal glutamate. J Am Chem Soc 132: 5610-5612
15. Wang T, Li H, Lin G, Tang C, Li D, Nathan C, Darwin KH, Li H (2009) Structural insights on the Mycobacterium tuberculosis proteasomal ATPase Mpa. Structure 17: 1377-1385
16. Wilkinson KD (2009) DUBs at a glance. J Cell Sci 122: 2325-2329