Proteasomes from structure to function: perspectives from Archaea.
Insight into the world of proteolysis has expanded considerably over the past decade. Energy-dependent proteases, such as the proteasome, are no longer viewed as nonspecific degradative enzymes associated solely with protein catabolism but are intimately involved in controlling biological processes that span life to death. The proteasome maintains this exquisite control by catalyzing the precisely timed and rapid turnover of key regulatory proteins. Proteasomes also interplay with chaperones to ensure protein quality and to readjust the composition of the proteome following stress. Archaea encode proteasomes that are highly related to those of eukaryotes in basic structure and function. Investigations of archaeal proteasomes coupled with those of eukaryotes has greatly facilitated our understanding of the molecular mechanisms that govern regulated protein degradation by this elaborate nanocompartmentalized machine.
Maupin-Furlow
Julie A
JA
Department of Microbiology and Cell Science, University of Florida Gainesville, Florida 32611, USA.
Humbard
Matthew A
MA
Kirkland
P Aaron
PA
Li
Wei
W
Reuter
Christopher J
CJ
Wright
Amy J
AJ
Zhou
G
G
D001105:Archaea / Q000737:chemistry* / Q000201:enzymology*; D019843:Archaeal Proteins / Q000737:chemistry* / Q000502:physiology*; D046988:Proteasome Endopeptidase Complex / Q000737:chemistry* / Q000502:physiology*; D013329:Structure-Activity Relationship
D019843:Archaeal Proteins; D046988:Proteasome Endopeptidase Complex