NDLI: Identification of an activation region in the proteasome activator REGα

Content Provider	PubMed Central
Author	Zhang, Zhiguo Clawson, Andrew Realini, Claudio Jensen, Christopher C. Knowlton, J. Randolph Hill, Christopher P. Rechsteiner, Martin
Copyright Year	1998
Abstract	Proteasomes can be markedly activated by associating with 19S regulatory complexes to form the 26S protease or by binding 11S protein complexes known as REG or PA28. Three REG subunits, α, β, and γ, have been expressed in Escherichia coli, and each recombinant protein can activate human proteasomes. Combining PCR mutagenesis with an in vitro activity assay, we have isolated and characterized 36 inactive, single-site mutants of recombinant REGα. Most are monomers that produce functional proteasome activators when mixed with REGβ subunits. Five REGα mutants that remain inactive in the mixing assay contain amino acid substitutions clustered between Arg-141 and Gly-149. The crystal structure of the REGα heptamer shows that this region forms a loop at the base of each REGα subunit. One mutation in this loop (N146Y) yields a REGα heptamer that binds the proteasome as tightly as wild-type REGα but does not activate peptide hydrolysis. Corresponding amino acid substitutions in REGβ (N135Y) and REGγ (N151Y) produce inactive proteins that also bind the proteasome and inhibit proteasome activation by their normal counterparts. Our studies clearly demonstrate that REG binding to the proteasome can be separated from activation of the enzyme. Moreover, the dominant negative REGs identified here should prove valuable for elucidating the role(s) of these proteins in antigen presentation.
Starting Page	2807
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	6
Volume Number	95
Language	English
Publisher	The National Academy of Sciences
Publisher Date	1998-03-17
Access Restriction	Open
Rights Holder	The National Academy of Sciences
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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