The post-translational modification (PTM) of proteins plays a critical role in the regulation of
a broad range of cellular processes in eukaryotes. Yet their role in governing similar systems …

Posttranslational modifications in the form of covalently attached proteins like ubiquitin (Ub),
were long considered an exclusive feature of eukaryotic organisms. The discovery of …

Pupylation, a post-translational modification found in Mycobacterium tuberculosis and other
Actinobacteria, involves the covalent attachment of prokaryotic ubiquitin-like protein (Pup) to …

One of several roles of the Mycobacterium tuberculosis proteasome is to defend against host-
produced nitric oxide (NO), a free radical that can damage numerous biological …

Intracellular protein degradation is an essential process in all life domains. While in all
eukaryotes regulated protein degradation involves ubiquitin tagging and the 26S …

Proteasomal protein degradation exists in mycobacteria and other actinobacteria, and
expands their repertoire of compartmentalizing protein degradation pathways beyond the …

Pupylation is a post-translational protein modification occurring in actinobacteria through
which the small, intrinsically disordered protein Pup (prokaryotic ubiquitin-like protein) is …

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 …

The balance of sufficient iron supply and avoidance of iron toxicity by iron homeostasis is a
prerequisite for cellular metabolism and growth. Here we provide evidence that, in …

The bacterial cytosol is a complex mixture of macromolecules (proteins, DNA, and RNA),
which collectively are responsible for an enormous array of cellular tasks. Proteins are …