Archaeal proteasomes and other regulatory proteases.
Numerous proteases have been shown to catalyze the precisely-timed and rapid turnover of key cellular proteins. Often these regulatory proteases are either energy-dependent or intramembrane-cleaving. In archaea, two different types of energy-dependent proteases have been characterized: 20S proteasomes associated with proteasome-activating nucleotidases and membrane-associated Lon proteases. Interestingly, homologs of all three mechanistic classes of intramembrane-cleaving proteases are widely distributed in archaea. Similar to their eucaryal and bacterial counterparts, members of these uncharacterized proteases might promote the controlled release of membrane-anchored regulatory proteins or liberate small peptide reporters and/or effectors that function in cell signaling.
Maupin-Furlow
Julie A
JA
Department of Microbiology and Cell Science, University of Florida, Gainesville, FL 32611-0700, USA. jmaupin@ufl.edu
Gil
Malgorzata A
MA
Humbard
Matthew A
MA
Kirkland
Phillip Aaron
PA
Li
Wei
W
Reuter
Christopher J
CJ
Wright
Amy J
AJ
D000595:Amino Acid Sequence; D001105:Archaea / Q000201:enzymology* / Q000235:genetics; D019843:Archaeal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D019848:Gene Expression Regulation, Archaeal; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D049070:Protease La / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D046988:Proteasome Endopeptidase Complex / Q000235:genetics / Q000378:metabolism*
D019843:Archaeal Proteins; D010447:Peptide Hydrolases; D049070:Protease La; D046988:Proteasome Endopeptidase Complex