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J Biol Chem, Vol. 274, Issue 37, 26008-26014, September 10, 1999
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From the In eukaryotes, the 20 S proteasome is the
proteolytic core of the 26 S proteasome, which degrades ubiquitinated
proteins in an ATP-dependent process. Archaebacteria lack
ubiquitin and 26 S proteasomes but do contain 20 S proteasomes. Many
archaebacteria, such as Methanococcus jannaschii, also
contain a gene (S4) that is highly homologous to the six
ATPases in the 19 S (PA700) component of the eukaryotic 26 S
proteasome. To test if this putative ATPase may regulate proteasome
function, we expressed it in Escherichia coli and purified
the 50-kDa product as a 650-kDa complex with ATPase activity. When
mixed with the well characterized 20 S proteasomes from
Thermoplasma acidophilum and ATP, this complex stimulated degradation of several unfolded proteins 8-25-fold. It also stimulated proteolysis by 20 S proteasomes from another archaebacterium and mammals. This effect required ATP hydrolysis since ADP and the nonhydrolyzable analog, 5'-adenylyl Department of Cell Biology, Harvard Medical
School, Boston, Massachusetts 02115 and the ¶ Institute for
Genomic Research, Rockville, Maryland 20850
,
-imidophosphate, were
ineffective. CTP and to a lesser extent GTP and UTP were also
hydrolyzed and also stimulated proteolysis. We therefore named this
complex PAN for proteasome-activating nucleotidase. However, PAN did
not promote the degradation of small peptides, which, unlike proteins,
should readily diffuse into the proteasome. This ATPase complex appears to have been the evolutionary precursor of the eukaryotic 19 S complex, before the coupling of proteasome function to ubiquitination.
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