Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9276542 | Current Opinion in Microbiology | 2005 | 9 Pages |
Abstract
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.
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Authors
Julie A Maupin-Furlow, Malgorzata A Gil, Matthew A Humbard, Phillip Aaron Kirkland, Wei Li, Christopher J Reuter, Amy J Wright,