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Annu Rev Microbiol. 2014;68:155-75. doi: 10.1146/annurev-micro-091313-103447. Epub 2014 May 29.

Prokaryotic ubiquitin-like protein modification.

Author information

1
Department of Microbiology and Cell Science, University of Florida, Gainesville, Florida 32611; email: jmaupin@ufl.edu.

Abstract

Prokaryotes form ubiquitin (Ub)-like isopeptide bonds on the lysine residues of proteins by at least two distinct pathways that are reversible and regulated. In mycobacteria, the C-terminal Gln of Pup (prokaryotic ubiquitin-like protein) is deamidated and isopeptide linked to proteins by a mechanism distinct from ubiquitylation in enzymology yet analogous to ubiquitylation in targeting proteins for destruction by proteasomes. Ub-fold proteins of archaea (SAMPs, small archaeal modifier proteins) and Thermus (TtuB, tRNA-two-thiouridine B) that differ from Ub in amino acid sequence, yet share a common β-grasp fold, also form isopeptide bonds by a mechanism that appears streamlined compared with ubiquitylation. SAMPs and TtuB are found to be members of a small group of Ub-fold proteins that function not only in protein modification but also in sulfur-transfer pathways associated with tRNA thiolation and molybdopterin biosynthesis. These multifunctional Ub-fold proteins are thought to be some of the most ancient of Ub-like protein modifiers.

KEYWORDS:

TtuB; molybdopterin; pupylation; sampylation; sulfur; tRNA thiolation

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