Progress in the study of prokaryotic ubiquitin-like protein (Pup) - Proteasome system

Progress in Biochemistry and Biophysics

Volumn 38, Issue 12, 2011, Pages 1091-1098

  Wang, Chun Jun ^a   Lin, Jin ^b   Zhang, Jun Jie ^b  

^a BEIJING FORESTRY UNIVERSITY   (China)

^b BEIJING NORMAL UNIVERSITY   (China)

Author keywords

Mycobacterium tuberculosis; Prokaryotic ubiquitin like protein (Pup); Proteasome; Protein degradation

Indexed keywords

ACTINOBACTERIA; ACTINOBACTERIA (CLASS); EUKARYOTA; MYCOBACTERIUM TUBERCULOSIS; PROKARYOTA;

EID: 84863258950     PISSN: 10003282     EISSN: None     Source Type: Journal    
DOI: 10.3724/SP.J.1206.2011.00110     Document Type: Article

References (45)

1. Knipfer N, Shrader T E. Inactivation of the 20S proteasome in Mycobacterium Smegmatis. Mol Microbio, 1997, 25(2):375-383 (Pubitemid 27351588)
2. Baumeister W, Walz J, Zu F, et al. The proteasome: Paradigm of a self-Compartmentalizing protease. Cell, 1998, 92(3):367-380 (Pubitemid 28093014)
3. Hu G, Lin G, Wang M, et al. Structure of the Mycobacterium tuberculosis proteasome and mechanism of inhibition by a peptidyl boronate. Mol Microbio, 2006, 59(5):1417-1428
4. Lin G, Hu G, Tsu C, et al. Mycobacterium tuberculosis prcBA genes encode a gated proteasome. Mol Microbio, 2006, 59(5):1405-1416
5. Lowe J, Stock D, Jap B, et al. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4Å resolution. Science, 1995, 268(5210):533-539
6. Lin G, Tsu C, Dick L, et al. Distinct specificities of Mycobacterium tuberculosis and mammalian proteasomes for N-Acetyl tripeptide substrates. J Biol Chem, 2008, 283(49):34423-34431
7. Wolf S, Nagy I, Lupas A, et al. Characterization of ARC, a divergent member of the AAA ATPase family from Rhodococcus erythropolis. J Biol Chem, 1998, 277(1):13-25 (Pubitemid 28151880)
8. Darwin K H, Ehrt S, Gutierrez-Ramos J C, et al. The proteasome of Mycobacterium tuberculosis is required for resistance to nitric oxide. Science, 2003, 302(12):1963-1966 (Pubitemid 37523503)
9. Pearce M J, Arora P, Festa R A, et al. Identification of substrates of the Mycobacterium tuberculosis proteasome. EMBO J, 2006, 25(22):5423-5432 (Pubitemid 44764151)
10. Darwin K H, Lin G, Chen Z, et al. Characterization of a Mycobacterium tuberculos is proteasomal ATPase homologue. Mol Microbio, 2005, 55(2):561-571 (Pubitemid 40179387)
11. Wang T, Darwin K H, Tang C Y, et al. Structural insights on the Mycobacterium tuberculosis proteasomal ATPase Mpa. Structure, 2009, 17(10):1279-1285
12. Li D, Li H L, Wang T, et al. Structural basis for the assembly and gate closure mechanisms of the Mycobacterium tuberculosis 20S proteasome. EMBO J, 2010, 29(12):2037-2047
13. Pearce M J, Mintseris J, Ferreyra J, et al. Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis. Science, 2008, 322(5904):1104-1107
14. Hershko, Ciechanover. The ubiquitin system. Nature Medicine, 2000, 6(10):1073-1081
15. Chen X, Solomon W C, Kang Y, et al. Prokaryotic ubiquitin-like protein Pup is intrinsically disordered. J Mol Biol, 2009, 392(1):208-217
16. Sutter M, Striebel F, Damberger F F, et al. A distinct structural region of the prokaryotic ubiquitin-like protein (Pup) is recognized by the N-terminal domain of the proteasomal ATPase Mpa. FEBS Letters, 2009, 583(19):3151-3157
17. Wang T, Darwin K H, Li H L, et al. Binding-induced folding of prokaryotic ubiquitin-like protein on the Mycobacterium proteasomal ATPase targets substrates for degradation. Nat Stru Mol Biol, 2010, 17(11):1352-1357
18. Burns K E, Pearce M J, Darwin K H, et al. Prokaryotic ubiquitinlike protein provides a two-part degron to Mycobacterium proteasome substrates. J Bacteriol, 2010, 192(11):2933-2935
19. Striebel F, Imkamp F, Sutter M, et al. Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes. Nat Stru Mol Biol, 2009, 16(6):647-651
20. Cerda-Maira F A, Pearce M J, Fuortes M, et al. Molecular analysis of theprokaryotic ubiquitin-like protein (Pup) conjugation pathway in Mycobacterium tuberculosis. Mol Microbio, 2010, 77(5):1123-1135
21. Imkamp F, Rosenberger T, Striebel F, et al. Deletion of dop in Mycobacterium smegmatis abolishes pupylation of protein substrates in vivo. Mol Microbio, 2010, 75(3):744-754
22. Burns A E, Cerda-Maira F A, Wang T, et al. "Depupylation" of prokaryotic ubiquitin-like protein from Mycobacterial proteasome substrates. Mol Cell, 2010, 39(5):821-827
23. Imkamp F, Striebel F, Sutter M, et al. Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway. EMBO Rep, 2010, 11(10):791-797
24. Iyer L, Burroughs A M, Aravind L. Unraveling the biochemistry and provenance of pupylation: a prokaryotic analog of ubiquitination. Biology Direct, 2008, 3(6150):45-52
25. Guth E, Thommen M, Weber-Ban E. Mycobacterial ubiquitin-like protein ligase PafA follows a two-step reaction pathway with a phosphorylated Pup intermediate. J Biol Chem, 2011, 286(6):4212-4219
26. Festa R A, Pearce M J, Darwin K H. Characterization of the proteasome accessory factor (paf) operon in Mycobacterium tuberculosis. J Bacteriol, 2007, 189(8):3044-3050 (Pubitemid 46697393)
27. Festa R A, McAllister F, Pearce M J, et al. Prokayrotic ubiquitinlike protein (Pup) proteome of Mycobacterium tuberculosis. PLoS ONE, 2010, 5(1): e8589
28. Watrous J, Burns K E, Liu W T, et al. Expansion of the mycobacterial "PUPylome". Molecular Bio Systems, 2010, 6(22):376-385
29. Kremer L, Nampoothiri K M, Lesjean S, et al. Biochemical characterization of acyl carrier protein (AcpM) and malonyl-CoA: AcpM transacylase (mtFabD), two major components of Mycobacterium tuberculosis fatty acid synthase II. J Biol Chem, 2001, 276(30):27967-27974
30. Sambandamurthy V K, Wang X, Chen B, et al. A pantothenate auxotroph of Mycobacterium tuberculosis is highly attenuated and protects mice against tuberculosis. Nat Med, 2002, 8(10):1171-1174 (Pubitemid 35175974)
31. Harth G, Horwitz M A. Export of recombinant Mycobacterium tuberculosis superoxide dismutase is dependent upon both information in the protein and mycobacterial export machinery. A model for studying export of leaderless proteins by pathogenic mycobacteria. J Biol Chem, 1999, 274(7):4281-4292
32. Burns K E, Liu W T, Boshoff H I M, et al. Proteasomal protein degradation in Mycobacteria is dependent upon a prokaryotic ubiquitin-like protein. J Biol Chem, 2008, 284(5):3069-3075
33. Movahedzadeh F, Smith D A, Norman R A, et al. The Mycobacterium tuberculosis ino1 gene is essential for growth and virulence. Mol Microbio, 2004, 51(4):1003-1014 (Pubitemid 38270795)
34. Honer Zu Bentrup K, Miczak A, Swenson D L, et al. Characterization of activity and expression of isocitrate lyase in Mycobacterium avium and Mycobacterium tuberculosis. J Bacteriol, 1999, 181(23):7661-7667
35. Fol M, Chauhan A, Niar N K, et al. Modulation of Mycobacterium tuberculosis proliferation by MtrA, an essential two-component response regulator. Mol Microbio, 2006, 60(3):643-657
36. Deshaies R J, Joazeiro C A P. RING domain E3 ubiquitin ligases. Biochemistry, 2009, 78(1):399-434
37. Wickliffe K, Williamson A, Jin L Y, et al. The multiple layers of ubiquitin-dependent cell cycle control. Chem Rev, 2009, 109(4):1537-1548
38. Gandotra S, Lebron M B, Ehrt S. The Mycobacterium tuberculosis proteasome active site threonine is essential for persistence yet dispensable for replication and resistance to nitric oxidea. PLoS Pathogens, 2010, 6(8): e1001040
39. Nathan C, Shiloh M U. Reactive oxygen and nitrogen intermediates in the relationship between mammalian hosts and microbial pathogens. Proc Natl Acad Sci USA, 2000, 97(16):8841-8848 (Pubitemid 30626635)
40. Gandotra S, Schnappinger D, Monteleone M, et al. In vivo gene silencing identifies the Mycobacterium tuberculosis proteasome as essential for the bacteria to persist in mice. Nat Med, 2007, 13(12):1515-1520 (Pubitemid 350224249)
41. Lamichhane G, Raghunand T R, Morroson N E, et al. Deletion of a Mycobacterium tuberculosis proteasomal ATPase homologue gene produces a slow-growing stain that persistFs in host tissues. J Infec Disea, 2006, 194(9):1233-1240 (Pubitemid 44630968)
42. Mitchison D A. Tuberculosis hits back. Nature, 2004, 427(22):295
43. Ginsberg A M, Spigelman M. Challenges in tuberculosis drug research and development. Nature Medicine, 2007, 13(3):290-294 (Pubitemid 46376672)
44. Lin G, Li D Y, Carvalho L P S, et al. Inhibitors selective for mycobacterial versus human proteasomes. Nature, 2009, 464(1):621-626
45. Lin G, Li D Y, Chidawanyika, et al. Fellutamide B is a potent inhibitor of the Mycobacterium tuberculosis proteasome. Arch Biochem Biopyhs, 2010, 501:214-220