Molecular organization of a high molecular weight multi-protease complex from rat liver

Tanaka, Keiji; Yoshimura, Teizo; Ichihara, Akira; Ikai, Atsushi; Nishigai, Masaaki; Morimoto, Yukio; Sato, Mamoru; Tanaka, Nobuo; Katsube, Yukiteru; Kameyama, Keiichi; Takagi, Toshio

doi:10.1016/0022-2836(88)90123-4

Cited by 114 publications

(114 citation statements)

References 31 publications

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“…The high degree of conservation between regions of these subunits from Drosophila (PROS-35) and rat (C2) is interesting and consistent with earlier observations that multicatalytic proteinase complexes, even from widely different species, show some antigenic cross-reactivity on Western blots [2,10,11,21]. A search of the National Biomedical Research Foundation (NBRF, 1313189) and SWISSPROT (1013189) protein sequence data bases has revealed no obvious sequence similarity between the N-terminal sequences of multicatalytic proteinase subunits and any other proteins.…”

Section: Resultssupporting

confidence: 87%

N‐Terminal sequence similarities between components of the multicatalytic proteinase complex

1990

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The multicatalytic proteinase complex is a high molecular weight nonlysosomal proteinase which is composed of many different types of subunit. As part of a study of the possible relationships between subunits, polypeptides derived from the multicatalytic proteinase from rat liver have been subjected to N-terminal amino acid sequence analysis. Although several of the subunits are blocked at their N-termini, sequences have been obtained for 7 of the polypeptides. Each of the 7 sequences is unique but they show considerable sequence similarity, suggesting that the proteins are encoded by members of the same gene family.Multicatalytic proteinase.; Protease; Gene family; (Rat liver)

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Section: Resultssupporting

confidence: 87%

N‐Terminal sequence similarities between components of the multicatalytic proteinase complex

1990

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“…C-Subset looks very much like one of the characteris-tic views of 20 S proteasome once suggested as a dimeric aggregate of disk-like proteasome [6]. More recent interpretations, however, tend to present it as the side view of cylindrical proteasome itself [7,8].…”

Section: Resultsmentioning

confidence: 95%

Electron microscopy of 26 S complex containing 20 S proteasome

et al. 1991

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A high molecular weight protease complex (26 S complex) involved in the intracellular protein degradation of ubiquitinated proteins was purified from rat liver and studied by electron microscopy. The most prevalent molecular species with best preserved symmetrical morphology had two large rectangular terminal structures attached to a thinner central one having four protein layers. We concluded that they were the closest representation of the 26 S complex so far reported. The central structure was identified as 20 S proteasome and the terminal one as recognition units for ubiquitinated proteins.

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“…Proteasomes, also called large multicatalytic protease complexes, are 20 S ring-shaped particles consisting of multiple, non-identical subunits with sizes ranging from 22 to 33 kDa [1,2]. They contain at least three distinct catalytic sites, that are specific for the hydrolyses of various proteins and hydrophobic, basic and acidic peptides and have neutral or alkaline pH optima [ 1,2].…”

Section: Introductionmentioning

confidence: 99%

“…They contain at least three distinct catalytic sites, that are specific for the hydrolyses of various proteins and hydrophobic, basic and acidic peptides and have neutral or alkaline pH optima [ 1,2]. These protease activities appear to be present in a latent form because purified proteasomes can be activated by polylysine, fatty acids or SDS [1, 3,4].…”

Section: Introductionmentioning

confidence: 99%

Na⁺, K⁺‐specific inhibition of protein and peptide hydrolyses by proteasomes from human hepatoma tissues

Seol

Park

et al. 1989

FEBS Letters

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Proteasomes were purified from human hepatoma tissues, and their sensitivities to Na+ and K+ were examined. At concentrations of 10 mM or more, these cations were found to inhibit completely polylysine-activated casein degradation by the purified proteasomes. They also strongly inhibited the hydrolyses of peptides, although to a lesser extent. On the other hand, they reversed the inhibitory and stimulatory effects of polylysine on the hydrolyses of Sue-Leu-Tyr-AMC and Cbz-Ala-Arg-Arg-MNA, respectively. These results suggest that Na+ and/or K+ may be involved in the regulation of intracellular protein breakdown by controlling the multicatalytic activity of proteasomes.

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Molecular organization of a high molecular weight multi-protease complex from rat liver

Cited by 114 publications

References 31 publications

N‐Terminal sequence similarities between components of the multicatalytic proteinase complex

N‐Terminal sequence similarities between components of the multicatalytic proteinase complex

Electron microscopy of 26 S complex containing 20 S proteasome

Na⁺, K⁺‐specific inhibition of protein and peptide hydrolyses by proteasomes from human hepatoma tissues

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Molecular organization of a high molecular weight multi-protease complex from rat liver

Cited by 114 publications

References 31 publications

N‐Terminal sequence similarities between components of the multicatalytic proteinase complex

N‐Terminal sequence similarities between components of the multicatalytic proteinase complex

Electron microscopy of 26 S complex containing 20 S proteasome

Na+, K+‐specific inhibition of protein and peptide hydrolyses by proteasomes from human hepatoma tissues

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Product

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Na⁺, K⁺‐specific inhibition of protein and peptide hydrolyses by proteasomes from human hepatoma tissues