As the endpoint for the ubiquitin-proteasome system, the 26S proteasome is the principal
proteolytic machine responsible for regulated protein degradation in eukaryotic cells. The …

Polyubiquitination is a posttranslational modification where ubiquitin chains containing
isopeptide bonds linking one of seven ubiquitin lysines with the C terminus of an adjoining …

Type II topoisomerases disentangle DNA to facilitate chromosome segregation, and
represent a major class of therapeutic targets. Although these enzymes have been studied …

The assembly of bacterial toxins and virulence factors is critical to their function, but the
regulation of assembly during infection has not been studied. We begin to address this question …

The Polycomb repressive complex 1 (PRC1) mediates gene silencing, in part by monoubiquitination
of histone H2A on lysine 119 (uH2A). Bmi1 and Ring1b are critical components of …

The 26S proteasome is the principal macromolecular machine responsible for protein
degradation in eukaryotes. However, little is known about the detailed kinetics and coordination of …

Polyubiquitination is an essential posttranslational modification that plays critical roles in
cellular signaling. PolyUb (polyubiquitin) chains are formed by linking the carboxyl-terminus of …

Cdc48/p97 is an essential and highly conserved AAA+ ATPase that uses its protein-unfoldase
activity to extract ubiquitinated polypeptides from macromolecular complexes and …

Poly-ubiquitin chains direct protein substrates to the 26S proteasome, where they are
removed by the deubiquitinase Rpn11 during ATP-dependent substrate degradation. Rapid …

The complexity of protein ubiquitination signals derives largely from the variety of
polyubiquitin linkage types that can modify a target protein, each imparting distinct functional …