NDLI: Properties of the hybrid form of the 26S proteasome containing both 19S and PA28 complexes.

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Properties of the hybrid form of the 26S proteasome containing both 19S and PA28 complexes.

Content Provider	Semantic Scholar
Author	Cascio, Paolo Call, Matthew E. Walz, Thomas Goldberg, Alfred L.
Copyright Year	2002
Abstract	PA28 is a gamma-interferon-induced complex that associates with the 20S proteasome and stimulates breakdown of small peptides. Recent immunoprecipitation studies indicate that, in vivo, PA28 also exists in larger complexes that also contain the 19S particle, which is required for ATP-ubiquitin-dependent degradation of proteins. However, because of its lability, the structure and properties of this larger complex remain unclear. Here, we demonstrate that, in vitro, PA28 can associate with 'singly capped' 26S (i.e. 19S-20S) proteasomes. Electron microscopy of the resulting structures revealed one PA28 ring at one end of the 20S particle and a 19S complex at the other. These hybrid complexes show enhanced hydrolysis of small peptides, but no significant increase in rates of protein breakdown. Nevertheless, during breakdown of proteins, the complexes containing PA28alphabeta or PA28alpha generated a pattern of peptides different from those generated by 26S proteasomes, without altering mean product length. Presumably, this change in peptides produced accounts for the capacity of PA28 to enhance antigen presentation.
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://walz.med.harvard.edu/Publications/PDFs/Cascio-EMBO-2002.pdf
PubMed reference number	12032076v1
Volume Number	21
Issue Number	11
Journal	The EMBO journal
Language	English
Access Restriction	Open
Subject Keyword	19s 26S proteasome location Adenosine Triphosphate Antigen Presentation Catabolism Interferon Type II Large PSME1 gene Protein Degradation, Regulatory Recombinant Interferon-gamma multicatalytic endopeptidase complex proteasome activator complex location
Content Type	Text
Resource Type	Article

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