AAA+ family proteolytic machines (ClpXP, ClpAP, ClpCP, HslUV, Lon, FtsH, PAN/20S, and
the 26S proteasome) perform protein quality control and are used in regulatory circuits in all …

The 26S proteasome is a highly conserved protein degradation machine that consists of the
20S proteasome and 19S regulatory particles, which include 14 and 19 different …

▪ Abstract Proteasomes are large multisubunit proteases that are found in the cytosol, both
free and attached to the endoplasmic reticulum, and in the nucleus of eukaryotic cells. Their …

The final destination of the majority of proteins that have to be selectively degraded in
eukaryotic cells is the proteasome, a highly sophisticated nanomachine essential for life …

Proteins, with their seemingly limitless functional diversity, are major players in the
maintenance of life. The ability of proteins to fulfill these various biological functions is …

Escherichia coli ClpX, a member of the Clp family of ATPases, has ATP-dependent
chaperone activity and is required for specific ATP-dependent proteolytic activities …

Saccharomyces cerevisiae Hsp104, a hexameric member of the Hsp100/Clp subfamily of
AAA+ ATPases with two nucleotide binding domains (NBD1 and 2), refolds aggregated …

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 …

This map is an update of the edition 9 map by Berlyn et al.(MKB Berlyn, KB Low, and KE
Rudd, p. 1715–1902, in FC Neidhardt et al., ed., Escherichia coli and Salmonella: cellular …

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 …