Ontology highlight
ABSTRACT:
SUBMITTER: Maupin-Furlow JA
PROVIDER: S-EPMC4757901 | biostudies-literature | 2014
REPOSITORIES: biostudies-literature
Annual review of microbiology 20140529
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) ...[more]