ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation - PubMed (original) (raw)
ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation
Nadia Benaroudj et al. Mol Cell. 2003 Jan.
Free article
Abstract
To clarify the role of ATP in proteolysis, we studied archaeal 20S proteasomes and the PAN (proteasome-activating nucleotidase) regulatory complex, a homolog of the eukaryotic 19S ATPases. PAN's ATPase activity was stimulated similarly by globular (GFPssrA) and unfolded (casein) substrates, and by the ssrA recognition peptide. Denaturation of GFPssrA did not accelerate its degradation or eliminate the requirement for PAN and ATP. During degradation of one molecule of globular or unfolded substrates, 300-400 ATP molecules were hydrolyzed. An N-terminal deletion in the 20S alpha subunits caused opening of the substrate-entry channel and rapid degradation of unfolded proteins without PAN; however, degradation of globular GFPssrA still required PAN's ATPase activity, even after PAN-catalyzed unfolding. Thus, substrate binding activates ATP hydrolysis, which promotes three processes: substrate unfolding, gate opening in the 20S, and protein translocation.
Comment in
- Dissecting various ATP-dependent steps involved in proteasomal degradation.
Ogura T, Tanaka K. Ogura T, et al. Mol Cell. 2003 Jan;11(1):3-5. doi: 10.1016/s1097-2765(03)00004-2. Mol Cell. 2003. PMID: 12535513
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