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Prokaryotic ubiquitin-like protein modification.

Julie A Maupin-Furlow1

  • 1Department of Microbiology and Cell Science, University of Florida, Gainesville, Florida 32611;

Annual Review of Microbiology
|July 5, 2014
PubMed
Summary

Prokaryotes utilize ubiquitin-like proteins for essential cellular functions, including protein modification and targeting for degradation. These ancient Ub-fold proteins, like Pup and SAMPs, exhibit diverse roles beyond simple protein tagging.

Keywords:
TtuBmolybdopterinpupylationsampylationsulfurtRNA thiolation

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Area of Science:

  • Biochemistry and Molecular Biology
  • Microbiology
  • Structural Biology

Background:

  • Prokaryotes employ ubiquitin (Ub)-like proteins to form isopeptide bonds with lysine residues via distinct, regulated pathways.
  • Ubiquitylation, a key process, targets proteins for proteasomal degradation.
  • Alternative Ub-like proteins exist in prokaryotes, differing in sequence but sharing a conserved β-grasp fold.

Purpose of the Study:

  • To elucidate the distinct mechanisms of Ub-like protein modification in prokaryotes.
  • To investigate the functional roles of Ub-fold proteins beyond protein modification.
  • To explore the evolutionary origins and ancient nature of Ub-like protein modifiers.

Main Methods:

  • Comparative analysis of Ub-like protein modification pathways in different prokaryotic organisms (e.g., mycobacteria, archaea, Thermus).
  • Enzymological characterization of Pup, SAMPs, and TtuB conjugation mechanisms.
  • Structural comparison of Ub-fold proteins to understand conserved structural motifs.

Main Results:

  • Mycobacteria use Pup for protein modification via a pathway distinct from ubiquitylation, targeting proteins for proteasomal degradation.
  • Archaea (SAMPs) and Thermus (TtuB) utilize Ub-fold proteins to form isopeptide bonds through streamlined mechanisms.
  • SAMPs and TtuB are multifunctional, involved in both protein modification and essential sulfur-transfer pathways (tRNA thiolation, molybdopterin biosynthesis).

Conclusions:

  • Prokaryotic Ub-like protein modification systems are diverse and employ unique enzymatic strategies.
  • Certain Ub-fold proteins are ancient and multifunctional, playing critical roles in fundamental cellular processes.
  • These findings highlight the evolutionary versatility of the Ub-fold and its ancient origins in prokaryotic biology.