Prokaryotic ubiquitin-like protein

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Prokaryotic Ubiquitin-Like Protein (Pup)
Prokaryotic Ubiquitin-Like Protein (Pup)
Three prokaryotic ubiquitin-like proteins (blue) bound to the proteasomal ATPase Mpa (red)

Existing structural data : 3M91 , 3M9D

Mass / length primary structure 6.944 kDa / 64 amino acids
Identifier
Gene name (s) Pup / Mpa PDB: 3M9D
External IDs
Occurrence
Parent taxon Prokaryotes

The prokaryotic ubiquitin-like protein (in German about 'prokaryotic ubiquitin-like protein', Pup) is a small, mostly unstructured protein with a function similar to ubiquitin . In contrast to ubiquitin, pup occurs only in prokaryotes and here mainly in actinobacteria such as Mycobacterium tuberculosis . Just like ubiquitin, Pup is also specifically ligated to the lysine of a protein as a post-translational modification , although only two enzymes , Dop and PafA , are required. In a first step, the Deamidase Dop converts the C-terminal glutamine into glutamic acid in order to activate Pup into a substrate for the second enzyme, PafA. PafA then establishes an isopeptide bond between Pup and a substrate lysine, depending on the ATP . The process is known as pupylation . Pupylated substrates are bound by the mycobacterial proteasomal ATPase ( Mpa ) in that Pup forms a binding-induced α-helix . Mpa then delivers the Pup-labeled protein to the 20S core particle, thereby degrading the substrate. The interaction of Pup, the two enzymes Dop and PafA, and the protease is also known as the prokaryotic proteasomal system (PPS).

structure

The amino acid sequence for Pup from Mycobacterium tuberculosis in one -letter code - highlighted with the C-terminal glutamine bold -: 

N-Terminus MAQEQTKRGGGGGDDDDIAGSTAAGQERREKLTEETDDLLDEIDDVLEENAEDFVRAYVQKGGQ C-Terminus

See also

Individual evidence

  1. ↑ Kristin E. Burns, Wei-Ting Liu, Helena IM Boshoff, Pieter C. Dorrestein, Clifton E. Barry: Proteasomal Protein Degradation in Mycobacteria Is Dependent upon a Prokaryotic Ubiquitin-like Protein . In: Journal of Biological Chemistry . 284, No. 5, 2009, ISSN  0021-9258 , pp. 3069-3075. doi : 10.1074 / jbc.M808032200 .
  2. ↑ Frank Striebel, Frank Imkamp, ​​Dennis Özcelik, Eilika Weber-Ban: Pupylation as a signal for proteasomal degradation in bacteria . In: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research . 1843, No. 1, 2014, ISSN  0167-4889 , pp. 103-113. doi : 10.1016 / j.bbamcr.2013.03.022 .
  3. ↑ Tao Wang, K. Heran Darwin, Huilin Li: Binding-induced folding of prokaryotic ubiquitin-like protein on the Mycobacterium proteasomal ATPase targets substrates for degradation . In: Nature Structural & Molecular Biology . 17, No. 11, 2010, ISSN  1545-9993 , pp. 1352-1357. doi : 10.1038 / nsmb.1918 .
  4. ↑ Michael J. Pearce, Julian Mintseris, J. Ferreyra, SP Gygi, K. Heran Darwin: Ubiquitin-Like Protein Involved in the Proteasome Pathway of Mycobacterium tuberculosis . In: Science . 322, No. 5904, 2008, ISSN  0036-8075 , pp. 1104-1107. doi : 10.1126 / science.1163885 .
  5. ↑ UniProt P9WHN4