Proteasomes (multi-protease complexes) as 20 S ring-shaped particles in a variety of eukaryotic cells.

Tanaka, Keiji; Yoshimura, Teizo; Kumatori, Atsushi; Ichihara, Akira; Ikai, Atsushi; Nishigai, Masaaki; Kameyama, Keiichi; Takagi, Toshio

doi:10.1016/s0021-9258(18)37580-x

Cited by 212 publications

(40 citation statements)

References 42 publications

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“…Western blotting was performed as described previously (Saeki et al, 2005) with the following antibodies: horseradish peroxidase-conjugated anti-Flag antibody (M2, Sigma), anti-ubiquitin antibody (P4D1, Santa Cruz Biotechnology, Santa Cruz, CA), anti-Rpt5 antibody (Affiniti Research), anti-Rpn5 antibody (Isono et al, 2007), and anti-CP antibody (Tanaka et al, 1988).…”

Section: Western Blottingmentioning

confidence: 99%

Multiple Proteasome-Interacting Proteins Assist the Assembly of the Yeast 19S Regulatory Particle

Saeki

Toh‐e

Kudo

et al. 2009

Cell

162

274

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The 26S proteasome is a highly conserved multisubunit protease that degrades ubiquitinated proteins in eukaryotic cells. The 26S proteasome consists of the proteolytic core particle (CP) and one or two 19S regulatory particles (RPs). Although the mechanisms of CP assembly are well described, the mechanism of RP assembly is largely unknown. Here, we show that four proteasome-interacting proteins (PIPs), Nas2/p27, Nas6/gankyrin, Rpn14/PAAF1, and Hsm3/S5b, bind specific Rpt subunits of the RP and interact each other genetically. Lack of these PIPs resulted in defective assembly of the 26S proteasome at an early stage, suggesting that these proteins are bona fide RP chaperones. Each of the RP chaperones formed distinct specific subassemblies of the base components and escorted them to mature RPs. Our results indicate that the RP assembly is a highly organized and elaborate process orchestrated by multiple proteasome-dedicated chaperones.

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Section: Western Blottingmentioning

confidence: 99%

Multiple Proteasome-Interacting Proteins Assist the Assembly of the Yeast 19S Regulatory Particle

Saeki

Toh‐e

Kudo

et al. 2009

Cell

162

274

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“…The proteasome has a molecular mass of •605 kD and is composed of 15-20 nonidentical protein subunits with molecular masses between 35 and 22 kD (Kloetzel et al, 1987;, which are encoded by an evolutionarily conserved gene family (Haass et al, 1990a;Tanaka 'et al, 1990). The proteasome has the appearance of a tripartite reel-shaped structure (Baumeister et al, 1988) and has been isolated from organisms as distant in evolution as archaebacteria, yeast, Drosophila, Xenopus, and man (Dahlmann et al, 1989b;Kremp et al, 1986;Kleinschmidt et al, 1988;Schuldt and Kloetzel, 1985;Arrigo et al, 1985;Akhayat et al, 1987;Kleinschmidt et al, 1983;Schmid et al, 1984;Tanaka et al, 1988). The enzyme is therefore thought to play an essential role in intracellular protein metabolism.…”

mentioning

confidence: 99%

Cell-specific accumulation of Drosophila proteasomes (MCP) during early development.

Klein

Gernold

Kloetzel

1990

The Journal of Cell Biology

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Abstract. The proteasome (MCP) is a high relative molecular mass multicatalytic proteinase complex composed of nonidentical protein subunits. We have investigated the cellular distribution of the enzyme complex during Drosophila embryogenesis using the proteasome specific antibodies N19-35 and N19-28 for immunocytology. Antibody staining of whole-mount embryos shows that during embryogenesis proteasomes are present in proliferating cells and that their accumulation and turnover is differentially regulated. Our data suggest that the proteasome may serve different proteolytic processes and that the enzyme may be involved in cell-specific proteolytic events required for cell proliferation and morphogenesis during early Drosophila development.

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“…These particles are unusual in that they contain several different enzymatic activities. In yeast, Drosophila, amphib-ian, chicken, and mammalian cells, these 19-S particles have multiple proteolytic activities and in the mammalian cells they have been shown to be identical to the prosome (Hough et al, 1987;Arrigo et al, 1988;Falkenburg et al, 1988;Tanaka et al, 1988). Each particle contains up to three different proteolytic activities, based upon the pH optima, substrate specificity, and the differential effects of inhibitors and activators (Tanaka et al, 1986;Hough et al, 1987).…”

mentioning

confidence: 99%

The sea urchin multicatalytic protease: purification, biochemical analysis, subcellular distribution, and relationship to snRNPs.

Grainger

Winkler

1989

The Journal of Cell Biology

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Abstract. We have purified and extensively characterized a 19-S particle from sea urchin eggs. This particle is the sea urchin homologue of the ~prosome", a particle originally identified in duck erythroblasts. We now show that these sea urchin prosomes contain multiple proteolytic activities. As shown for analogous particles from other cells, these particles hydrolyze synthetic substrates containing neutral hydrophobic or basic amino acids at the carboxy terminus of the synthetic peptides. They contain 16-20 small proteins ranging in molecular weight from 20,000 to 32,000. Peptide mapping shows that most of the polypeptides are unique, however, three exist in two isoelectric forms. We have investigated the possible function of the sea urchin multicatalytic proteases (MCPs) by determining their subcellular distribution, their relationship to egg snRNPs, and their possible role in translational repression. There are almost as many MCPs (2 x l0 s) as ribosomes (6.6 x l0 s) or mRNPs (1.8 x 107 ) per egg. This suggests that like ribosomes, the MCPs are stored in the egg for use during later development. We find that a substantial proportion of egg MCPs move into nuclei by the late blastula stage. Using a specific antibody against one of the sea urchin MCP proteins and antibodies against U1-U6, La, and Ro RNPs, we show that the sea urchin particle is distinct from these RNPs, although the anti-U1-U6 RNP antibody cross-reacts with a single MCP protein. In addition, the sea urchin MCP appears to be associated with a large structure in the cytoplasm of unfertilized eggs and is released under the same conditions that activate egg mRNPs in vitro.

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Proteasomes (multi-protease complexes) as 20 S ring-shaped particles in a variety of eukaryotic cells.

Cited by 212 publications

References 42 publications

Multiple Proteasome-Interacting Proteins Assist the Assembly of the Yeast 19S Regulatory Particle

Multiple Proteasome-Interacting Proteins Assist the Assembly of the Yeast 19S Regulatory Particle

Cell-specific accumulation of Drosophila proteasomes (MCP) during early development.

The sea urchin multicatalytic protease: purification, biochemical analysis, subcellular distribution, and relationship to snRNPs.

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