title: Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway.
abstract: Post-translational modification of proteins with prokaryotic ubiquitin-like protein (Pup) is the bacterial equivalent of ubiquitination in eukaryotes. Mycobacterial pupylation is a two-step process in which the carboxy-terminal glutamine of Pup is first deamidated by Dop (deamidase of Pup) before ligation of the generated γ-carboxylate to substrate lysines by the Pup ligase PafA. In this study, we identify a new feature of the pupylation system by demonstrating that Dop also acts as a depupylase in the Pup proteasome system in vivo and in vitro. Dop removes Pup from substrates by specific cleavage of the isopeptide bond. Depupylation can be enhanced by the unfolding activity of the mycobacterial proteasomal ATPase Mpa.
authors.affiliation: Department of Biology, Eidgenössische Technische Hochschule Zurich, Institute of Molecular Biology and Biophysics, Schafmattstrasse 20, Zurich CH-8093, Switzerland.
authors.forename: Frank
authors.initials: F
authors.lastname: Imkamp
authors.forename: Frank
authors.initials: F
authors.lastname: Striebel
authors.forename: Markus
authors.initials: M
authors.lastname: Sutter
authors.forename: Dennis
authors.initials: D
authors.lastname: Ozcelik
authors.forename: Natalie
authors.initials: N
authors.lastname: Zimmermann
authors.forename: Peter
authors.initials: P
authors.lastname: Sander
authors.forename: Eilika
authors.initials: E
authors.lastname: Weber-Ban
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism*; D005973:Glutamine / Q000378:metabolism; D008025:Ligases / Q000378:metabolism; D008239:Lysine / Q000378:metabolism; D009169:Mycobacterium tuberculosis / Q000235:genetics / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex / Q000235:genetics / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D014452:Ubiquitins / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; C533288:Pup protein, Mycobacterium tuberculosis; D014452:Ubiquitins; D005973:Glutamine; D046988:Proteasome Endopeptidase Complex; D008025:Ligases; D008239:Lysine
references.citation: Mol Microbiol. 1995 Jun;16(5):991-1000
references.pmid: 7476195
references.citation: Mol Microbiol. 2010 Feb;75(3):744-54
references.pmid: 20025664
references.citation: Nat Struct Mol Biol. 2009 Jun;16(6):647-51
references.pmid: 19448618
references.citation: Annu Rev Biochem. 2009;78:363-97
references.pmid: 19489724
references.citation: EMBO J. 2006 Nov 15;25(22):5423-32
references.pmid: 17082771
references.citation: Science. 2008 Nov 14;322(5904):1104-7
references.pmid: 18832610
references.citation: J Biol Chem. 2009 Jan 30;284(5):3069-3075
references.pmid: 19028679
references.citation: J Bacteriol. 2010 Jun;192(11):2933-5
references.pmid: 20233925
references.citation: J Cell Sci. 2009 Jul 15;122(Pt 14):2325-9
references.pmid: 19571111
references.citation: J Am Chem Soc. 2010 Apr 28;132(16):5610-2
references.pmid: 20355727
references.citation: Structure. 2009 Oct 14;17(10):1377-85
references.pmid: 19836337
references.citation: Biol Direct. 2008 Nov 03;3:45
references.pmid: 18980670
references.citation: Annu Rev Cell Dev Biol. 2006;22:159-80
references.pmid: 16753028
references.citation: Nature. 2010 Jan 7;463(7277):54-60
references.pmid: 20054389
references.citation: Annu Rev Biochem. 2009;78:477-513
references.pmid: 19489727
references.citation: EMBO J. 2010 Apr 7;29(7):1262-71
references.pmid: 20203624