Characterization of Two Polyubiquitin Binding Sites in the 26 S Protease Subunit 5a (Q28263609)

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proteasome endopeptidase complex

10 December 2024

main subject

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10 December 2024

author name string

P. Young

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Q. Deveraux

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R. E. Beal

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C. M. Pickart

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M. Rechsteiner

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http://www.jbc.org/content/273/10/5461.full.pdf

10 December 2024

publication date

6 March 1998

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language of work or name

English

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work available at URL

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https://api.elsevier.com/content/article/PII:S0021925818677968?httpAccept=text/xml

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https://api.elsevier.com/content/article/PII:S0021925818677968?httpAccept=text/plain

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https://syndication.highwire.org/content/doi/10.1074/jbc.273.10.5461

10 December 2024

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Journal of Biological Chemistry

10 December 2024

published in

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volume

273

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issue

10

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page(s)

5461-7

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cites work

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Arthrin, a myofibrillar protein of insect flight muscle, is an actin-ubiquitin conjugate

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Presence of protein A24 in rat liver nucleosomes

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Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis

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Site-specific phosphorylation of IkappaBalpha by a novel ubiquitination-dependent protein kinase activity

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A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein

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ATP-dependent incorporation of 20S protease into the 26S complex that degrades proteins conjugated to ubiquitin

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Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination

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Structure and functions of the 20S and 26S proteasomes

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Ubiquitin-dependent protein degradation

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How proteolysis drives the cell cycle

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A ubiquitin mutant with specific defects in DNA repair and multiubiquitination

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Yeast DNA Repair Proteins Rad6 and Rad18 Form a Heterodimer That Has Ubiquitin Conjugating, DNA Binding, and ATP Hydrolytic Activities

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Defective presentation to class I-restricted cytotoxic T lymphocytes in vaccinia-infected cells is overcome by enhanced degradation of antigen.

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Peptide antigen production by the proteasome: complexity provides efficiency

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UbcD1, a Drosophila ubiquitin-conjugating enzyme required for proper telomere behavior

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Surface hydrophobic residues of multiubiquitin chains essential for proteolytic targeting

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The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover.

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Inhibition of ubiquitin-mediated proteolysis by the Arabidopsis 26 S protease subunit S5a.

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Cloning and Sequencing a Non-ATPase Subunit of the Regulatory Complex of the Drosophila 26S Protease

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Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component of the 26S proteasome

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Molecular cloning and expression of a multiubiquitin chain binding subunit of the human 26S protease

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Rapid and efficient site-specific mutagenesis without phenotypic selection

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Rapid and efficient site-specific mutagenesis without phenotypic selection

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Novel Regulation of the Helix-Loop-Helix Protein Id1 by S5a, a Subunit of the 26 S Proteasome

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Mapping the ubiquitin‐binding domains in the p54 regulatory complex subunit of the Drosophila 26S protease

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A direct comparison of helix propensity in proteins and peptides

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Structure of tetraubiquitin shows how multiubiquitin chains can be formed

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Distinct 19 S and 20 S subcomplexes of the 26 S proteasome and their distribution in the nucleus and the cytoplasm

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Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85

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Novel multiubiquitin chain linkages catalyzed by the conjugating enzymes E2EPF and RAD6 are recognized by 26 S proteasome subunit 5

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Purification of two high molecular weight proteases from rabbit reticulocyte lysate

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KEKE motifs. Proposed roles in protein-protein association and presentation of peptides by MHC class I receptors

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