One of the most precisely regulated processes in living cells is intracellular protein
degradation. The main component of the degradation machinery is the 20S proteasome …

Folding of polypeptides in the cell typically requires the assistance of a set of proteins
termed molecular chaperones. Chaperones are an essential group of proteins necessary for …

HslUV is a" prokaryotic proteasome" composed of the HslV protease and the HslU ATPase,
a chaperone of the Clp/Hsp100 family. The 3.4 Å crystal structure of an HslUV complex is …

Background: The bacterial heat shock locus HslU ATPase and HslV peptidase together form
an ATP-dependent HslVU protease. Bacterial HslVU is a homolog of the eukaryotic 26S …

All organisms possess a diverse set of genetic programs that are used to alter cellular
physiology in response to environmental cues. The gram-negative bacterium Escherichia …

All organisms regulate cell cycle progression by coordinating cell division with DNA
replication status. In eukaryotes, DNA damage or problems with replication fork progression …

The ubiquitin/proteasome system serves as a regulated protein degradation pathway in
eukaryotes, and is involved in many cellular processes featuring high protein turnover rates …

HslVU is an ATP-dependent prokaryotic protease complex. Despite detailed crystal and
molecular structure determinations of free HslV and HslU, the mechanism of ATP-dependent …

HslVU is an ATP-dependent protease consisting of HslU ATPase and HslV peptidase. In an
HslVU complex, the central pores of HslU hexamer and HslV dodecamer are aligned and …

Protein turnover is critical for proteostasis, but turnover quantification is challenging, and
even in well-studied E. coli, proteome-wide measurements remain scarce. Here, we quantify …