Abstract：
:The eukaryotic 20S proteasome is known to associate with the IFN gamma-inducible regulator PA28. We analyzed the kinetics of product generation by 20S proteasomes with and without PA28. In the absence of PA28, the 20S proteasome rapidly generates peptides that have been cleaved only once, while internal fragments accumulate only slowly. In the presence of PA28, products generated by two flanking cleavages appear immediately as main products while the generation of single-cleavage products is strongly reduced. Kinetic data support a PA28-induced, coordinated double-cleavage mechanism. In particular, degradation of peptides derived from mouse cytomegalovirus pp89 and JAK1 kinase in the presence of PA28 leads to strongly enhanced production of the respective major histocompatibility complex ligands and potential precursors. These results show that PA28 profoundly alters the cleavage mechanism of the proteasome and appears to optimize the generation of dominant T-cell epitopes.
journal_name
Celljournal_title
Cellauthors
Dick TP,Ruppert T,Groettrup M,Kloetzel PM,Kuehn L,Koszinowski UH,Stevanović S,Schild H,Rammensee HGdoi
10.1016/s0092-8674(00)80097-5subject
Has Abstractpub_date
1996-07-26 00:00:00pages
253-62issue
2eissn
0092-8674issn
1097-4172pii
S0092-8674(00)80097-5journal_volume
86pub_type
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