PA700, an ATP-dependent activator of the 20 S proteasome, is an ATPase containing multiple members of a nucleotide-binding protein family.
George N. DeMartino,Carolyn R. Moomaw,Olga Zagnitko,Rita J. Proske,Ma Chu-Ping,Steven J. Afendis,Jonathan C. Swaffield,Clive A. Slaughter +7 more
TLDR
PA700 is composed of multiple members of a protein family that may function in the ATP-dependent regulation of proteasome activity, and treatment of PA700 with alkylating agents, such as N-ethylmaleimide, inhibited with similar kinetics both proteasomes activation and ATPase activity, suggesting that these two activities are functionally linked.About:
This article is published in Journal of Biological Chemistry.The article was published on 1994-08-19 and is currently open access. It has received 197 citations till now. The article focuses on the topics: Protein subunit & ATPase.read more
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The Ubiquitin-Proteasome Proteolytic Pathway: Destruction for the Sake of Construction
TL;DR: It is clear now that degradation of cellular proteins is a highly complex, temporally controlled, and tightly regulated process that plays major roles in a variety of basic pathways during cell life and death as well as in health and disease.
Journal ArticleDOI
The 26S Proteasome: A Molecular Machine Designed for Controlled Proteolysis
TL;DR: In eukaryotic cells, most proteins in the cytosol and nucleus are degraded via the ubiquitin-proteasome pathway, and the 26S proteasome is a 2-MDa molecular machine built from approximately 31 different subunits, which catalyzes protein degradation.
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Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution.
TL;DR: The three-dimensional structure of the proteasome from the archaebacterium Thermoplasma acidophilum has been elucidated by x-ray crystallographic analysis by means of isomorphous replacement and cyclic averaging.
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Mechanisms of mhc class i-restricted antigen processing
Eric G. Pamer,Peter Cresswell +1 more
TL;DR: A subset of the proteasome beta-subunits and one of the accessory complexes are upregulated by gamma-interferon and affect the generation of peptides to promote more efficient antigen recognition and bind lipid-based ligands within the endocytic pathway.
Journal ArticleDOI
Degradation of cell proteins and the generation of MHC class I-presented peptides.
TL;DR: Recent discoveries about the proteolytic systems that degrade cell proteins are reviewed, how the ubiquitin-proteasome pathway generates the peptides presented on MHC-class I molecules, and how this process is stimulated by immune modifiers to enhance antigen presentation are reviewed.
References
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Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes.
TL;DR: Small amounts of myoglobin, beta-lactoglobulin, and other proteins and peptides can be spotted or electroblotted onto polyvinylidene difluoride membranes, stained with Coomassie Blue, and sequenced directly, suggesting that PVDF membranes are superior supports for sequence analysis of picomole quantities of proteins purified by gel electrophoresis.
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The ubiquitin system for protein degradation
Avram Hershko,Aaron Ciechanover +1 more
TL;DR: The Ubiquitin-C-TERMINAL HYDROLASES study highlights the importance of knowing the carrier and removal status of these components in the preparation of the UBIQUITIN-MEDIATED DEGRADATION.
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Proteolysis, proteasomes and antigen presentation
TL;DR: Proteasomes are proteolytic complexes that degrade cytosolic and nuclear proteins and have been implicated in ATP-ubiquitin-dependent proteolysis and in the processing of intracellular antigens for cytolytic immune responses.
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A fusion protein required for vesicle-mediated transport in both mammalian cells and yeast
Duncan W. Wilson,Celeste A. Wilcox,Gregory C. Flynn,Ellson Y. Chen,Wun Jing Kuang,William J. Henzel,Marc R. Block,Marc R. Block,Axel Ullrich,Axel Ullrich,James E. Rothman +10 more
TL;DR: A protein sensitive toN-ethylmaleimide catalyses the fusion of transport vesicles with Golgi cisternae in a mammalian cell-free system and is equivalent to the SEC18 gene product of the yeast Saccharomyces cerevisiae, known to be essential for vesicle-mediated transport from the endoplasmic reticulum to the Golgi apparatus.
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ATP-binding site of adenylate kinase: mechanistic implications of its homology with ras-encoded p21, F1-ATPase, and other nucleotide-binding proteins
TL;DR: The MgATP binding site of adenylate kinase, located by a combination of NMR and x-ray diffraction, is near three protein segments that are homologous in sequence to segments found in other nucleotide-binding phosphotransferases, suggesting equivalent mechanistic roles of these segments in all of these proteins.