Abstract
Eukaryotic proteasomes are unusually large proteins with a heterogeneous subunit composition and have been classified into two isoforms with apparently distinct sedimentation coefficients of 20S and 26S. The 20S proteasome is composed of a set of small subunits with molecular masses of 21–32 kDa. The 26S proteasome is a multi-molecular assembly, consisting of a central 20S proteasome and two terminal subsets of multiple subunits of 28–112 kDa attached to the central part in opposite orientations. The primary structures of all the subunits of mammalian and yeast 20S proteasomes have been deduced from the nucleotide sequences of cDNAs or genes isolated by recombinant DNA techniques. These genes constitute a unique multi-gene family encoding homologous polypeptides that have been conserved during evolution. In contrast, little is yet known about the terminal structures of the 26S proteasome, but the cDNA clonings of those of humans are currently in progress. In this review, I summarize available information of the structural features on eukaryotic 20S and 26S proteasomes which has been clarified by molecular-biological methods.
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References
Orlowski M (1990) Biochemistry 29: 10289–10297
Rivett AJ (1993) Biochem J 291: 1–10
Goldberg AL (1992) Eur J Biochem 205: 9–23
Rechsteiner M, Hoffman L & Dubiel W (1993) J Biol Chem 268: 6065–6068
Hershko A & Ciechanover A (1992) Annu Rev Biochem 61: 761–807
Palombella VJ, Rando OJ, Goldberg AL & Maniatis T (1994) Cell 78: 773–785
Murakami Y, Matsufuji S, Kameji T, Hayashi S, Igarashi K, Tamura T, Tanaka K, Ichihara A (1992) Nature 360: 597–599
Goldberg AL & Rock KL (1992) Nature 357: 375–379
Ciechanover, A (1994) Cell 79: 13–21
Palombella VJ, Rando OJ, Goldberg AL & Maniatis T (1994) Cell 78: 773–785
Tanaka K, Yoshimura T, Ichihara A, Kameyama K & Takagi T (1986) J Biol Chem 261: 15204–15207
Tanaka K, Yoshimura T, Ichihara A, Ikai A, Nishigai M, Morimoto M, Sato M, Tanaka N, Katsube Y, Kameyama K & Takagi T (1988) J Mol Biol 203: 985–996
Yoshimura T, Kameyama K, Takagi T, Ikai A, Tokunaga F, Koide T, Tanahashi N, Tamura T, Cejka Z, Baumeister W, Tanaka K, Ichihara A (1993) J Struct Biol 111: 200–211
Lupas A, Kaster AJ & Baumeister W (1994) Enzyme Protein. in press
Kopp F, Dahlmann B & Hendil KB (1992) J Mol Biol 229: 14–19
Peters J-M, Cejka Z, Harris JR, Kleinschmidt JA & Baumeister W (1993) J Mol Biol 234: 932–937
Fujinami K, Tanahashi N, Tanaka K, Ichihara A, Cejka Z, Baumeister W, Miyawaki M, Sato T & Nakagawa H (1994) J Biol Chem 269: 25905–25910
Tanaka K, Tamura T, Yoshimura T & Ichihara A (1992) New Biol 4: 173–187
Tanahashi N, Tsurumi C, Tamura T & Tanaka K (1993) Enzyme Protein 47: 241–251
Hilt W, Heinemeyer W & Wolf DH (1994) in press
Heinemeyer W, Tröndle N, Albrecht G & Wolf DH (1994) Biochemistry 33: 12229–12237
Aki A, Shimbara N, Takashina M, Akiyama K, Kagawa S, Tamura T, Tanahashi N, Yoshimura T, Tanaka K & Ichihara A (1993) J Biochem 115: 257–269
Driscoll J, Brown MG, Finley D & Monaco JJ (1993) Nature 365: 262–264
Gaczynska M, Rock KL & Goldberg AL (1993) Nature 365: 264–267
Akiyama K, Kagawa S, Tamura T, Shimbara N, Takashina M, Hendil KB, Tanaka K & Ichihara A (1994) FEBS Lett 343: 85–88
Akiyama K, Yokota K, Kagawa S, Shimbara N, Tamura T, Akioka A, Nothwang HG, Noda C, Tanaka T & Ichihara A (1994) Science 265: 1231–1234
Tanaka K (1994) J Leukocyte Biol 56: 571–575
Orino E, Tanaka K, Tamura T, Sone S, Ogura T & Ichihara A (1991) FEBS Lett 284: 206–210
Kanayama H, Tamura T, Ugai S, Kagawa S, Tanahashi N, Yoshimura T, Tanaka K & Ichihara A (1992) Eur J Biochem 206: 567–578
Chu-Ping M, Vu JH, Proske RJ, Slaughter CA, DeMartino GN (1994) J Biol Chem 269: 3539–3547
Chu-Ping M, Slaughter CA & DeMartino GN (1994) J Biol Chem 267: 10515–10523
Armon T, Ganoth D & Hershko A (1990) J Biol Chem 265: 20723–6
Dubiel W, Pratt G, Ferrell K & Rechsteiner M (1992) J Biol Chem 267: 22369–22377
Shibuya H, Irie K, Ninomiya-Tsuji J & Matsumoto K (1992) Nature 357: 700–702
Dubiel W, Ferrell K & Rechsteiner M (1993) FEBS Lett 323: 276–278
Nelbock P, Dillon PJ, Perkins A & Rosen CA (1990) Science 248: 1650–1653.
Ohana B, Moore PA, Ruben SM, Southgate CD, Green MR & Rosen CA (1993) Proc Natl Acad Sci USA 90: 138–142
Akiyama Ket al., ms in prep.
Schnall R, Mannhaupt G, Stucka R, Tauer R, Ehnle S, Schwarzlose C, Vetter I & Feldmann H, (1994) Yeast 39: 1141–1155
Swaffield JC, Bromberg JF & Johnston SA (1992) Nature 357: 698–700
Kim Y-J, Björkund S, Li Y, Sayre MH & Kornberg RD (1994) Cell 77: 599–608
Dawson SP, Amond JE, Mayer NJ, Reynolds SE, Billett MA, Kloetzel PM, Tanaka K & Mayer RJ (1994) J Biol Chem in press
DeMartiono GN, Moomaw CR, Zagniko OP, Proske RJ, Chu-Ping M, Afendis SJ, Swaffield JC & Slaughter CA (1994) J Biol Chem 269: 10878–20884
Kominami K, Hisamatsu H, Tanahashi N, Shimizu Y, Tanaka K, Moomaw CR, Slaughter CA, DeMartino GN & Toh-e A (1994) EMBO J submitted
Nisogi H, Kominami K, Tanaka K & Toh-e A (1992) Exp Cell Res 200: 48–57
Ghisiain MS, Udvardy A & Mann C (1993) Nature 366: 358–362
Gordon C, McGurk G, Dillon P, Rosen C & Hastle N (1993) Nature 366: 355–357
Kominami Ket al., ms. in prep.
Tanaka Ket al., ms in prep.
Culbertson MR personal communication
Deveraux Q, Ustrell V, Pickart C & Rechsteiner M (1994) J Biol Chem 269: 7059–7061
Eytan E, Armon T, Heller H, Beck S & Hershko A (1993) J Biol Chem 268: 4668–4674
Ugai S, Tamura T, Tanahashi N, Takai S, Komi N, Chung CH, Tanaka K & Ichihara A (1993) J Biochem 113: 754–768
Realini C, Rogers SW & Rechsteier M (1994) FEBS Lett 348: 109–113
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Tanaka, K. Molecular biology of proteasomes. Mol Biol Rep 21, 21–26 (1995). https://doi.org/10.1007/BF00990966
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DOI: https://doi.org/10.1007/BF00990966