cDNA cloning and functional analysis of p28 (Nas6p) and p40.5 (Nas7p), two novel regulatory subunits of the 26S proteasome

Gene

Volumn 216, Issue 1, 1998, Pages 113-122

  Hori, Tomoko ^a   Kato, Seishi ^b   Saeki, Mihoro ^b   DeMartino, George N ^c   Slaughter, Clive A ^d   Takeuchi, Junko ^e   Toh e, Akio ^e   Tanaka, Keiji ^a  

^a JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^b SAGAMI CHEMICAL RESEARCH CENTER   (Japan)

^c UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^d HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^e UNIVERSITY OF TOKYO   (Japan)

Author keywords

26S proteasome; cDNA cloning; Gene disruption; Non ATPase subunit; p28 subunit; p40.5 subunit; PA700

Indexed keywords

ANKYRIN; COMPLEMENTARY DNA; PROTEASOME; PROTEIN; PROTEIN SUBUNIT; REGULATOR PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CELL PROLIFERATION; CELL VIABILITY; COMPUTER ANALYSIS; HUMAN; ISOELECTRIC POINT; MOLECULAR CLONING; MOLECULAR WEIGHT; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; YEAST; YEAST CELL;

ADENOSINE TRIPHOSPHATASES; AMINO ACID SEQUENCE; AMINO ACIDS; ANIMALS; BASE SEQUENCE; CATTLE; CELL DIVISION; CLONING, MOLECULAR; DNA, COMPLEMENTARY; ENDOPEPTIDASES; FUNGAL PROTEINS; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GENES, FUNGAL; HEAT; HUMANS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PEPTIDE HYDROLASES; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEINS; RNA, MESSENGER; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, DNA; SEQUENCE HOMOLOGY, AMINO ACID; TISSUE DISTRIBUTION; TUMOR CELLS, CULTURED;

EID: 0032541323     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(98)00309-6     Document Type: Article

References (33)

1. Baumeister, W., Walz, J., Zühl, F., Seemüller, E., 1998. The proteasome: paradigm of a self-compartmentalizing protease. Cell 92, 367-380.
2. Beyer, A., 1997. Sequence analysis of the AAA protein family. Protein Sci. 6, 2043-2058.
3. Blank, V., Kourisky, P., Israël, A., 1992. NF-kB and related proteins: Rel/dorsal homologies meet ankyrin-like repeats. Trends Biochem. Sci. 17, 135-140.
4. Coux, O., Tanaka, K., Goldberg, A.L., 1996. Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65, 801-847.
5. DeMartino, G.N., Moomaw, C.R., Zagnitko, O.P., Proske, R.J., Ma, C.-P., Afendis, S.J., Swaffield, J.C., Slaughter, C.A., 1994. PA700, an ATP-dependent activator of the 20S proteasome, is an ATPase containing multiple members of a nucleotide-binding protein family. J. Biol. Chem. 269, 20878-20884.
6. Dubiel, W., Ferrell, K., Rechsteiner, M., 1995. Subunits of the regulatory complex of the 26S protease. Mol. Biol. Rep. 21, 27-34.
7. Ferrell, K., Deveraux, Q., van Nocker, S., Rechsteiner, M., 1996. Molecular cloning and expression of a multiubiquitin chain binding subunit of the 26S protease. FEBS Lett. 381, 143-148.
8. Fujimuro, M., Tanaka, K., Yokosawa, H., Toh-e, A., 1998. Son1 is a component of the 26S proteasome of the yeast Saccharomyces cerevisiae. FEBS Lett. 423, 149-154.
9. Groll, M., Ditzel, L., Lowe, J., Stock, D., Bochtler, M., Bartunik, H.D., Huber, R., 1997. Structure of 20S proteasome from yeast at 2.4 A resolution. Nature 386, 463-471.
10. Hilt, W., Wolf, D.H., 1996. Proteasomes: destruction as a programme. Trends Biochem. Sci. 21, 96-102.
11. Hochstrasser, M., 1996. Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30, 405-439.
12. Ito, H., Fukuda, Y., Murata, K., Kimura, A., 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153, 163-168.
13. Johnson, E.S., Ma, P.C.M., Ota, I.M., Varshavsky, A., 1995. A proteolytic pathway that recognizes ubiquitin as a degradation signal. J. Biol. Chem. 270, 17442-17456.
14. Kato, S., Sekine, S., Oh, S.-W., Kim, N.-S., Umezawa, Y., Abe, N., Yokoyama-Kobayashi, M., Aoki, T., 1994. Construction of a human full-length cDNA bank. Gene 150, 243-250.
15. Kominami, K., DeMartino, G.N., Moomaw, C.R., Slaughter, C.A., Shimbara, N., Fujimuro, M., Yokosawa, H., Hisamatsu, H., Tanahashi, N., Shimizu, Y., Tanaka, K., Toh-e, A., 1995. Nin1p, a regulatory subunit of the 26S proteasome, is necessary for activation of Cdc28p kinase of Saccharomyces cerevisiae. EMBO J. 14, 3105-3115.
16. Kominami, K., Okura, N., Kawamura, M., DeMartino, G.N., Slaughter, C.A., Shimbara, N., Chung, C.H., Fujimuro, M., Yokosawa, H., Shimizu, Y., Tanahashi, N., Tanaka, K., Toh-e, A., 1997. Yeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multicopy supressors of nin1-1. Mol. Biol. Cell 8, 171-187.
17. Kozak, M., 1991. Structural features in eukaryotic mRNAs that modulate the initiation of translation. J. Biol. Chem. 266, 19867-19870.
18. Lam, Y.A., Xu, W., DeMartino, G.N., Cohen, R.E., 1997. Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome. Nature 385, 737-740.
19. Lõwe, J., Stock, D., Jap, B., Zwickl, P., Baumeister, W., Huber, R., 1995. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution. Science 268, 533-539.
20. Ma, C.-P., Vu, J.H., Proske, R.J., Slaughter, C.A., DeMartino, G.N., 1994. Identification, purification, and characterization of a high molecular weight, ATP-dependent activator (PA700) of the 20S proteasome. J. Biol. Chem. 269, 3539-3547.
21. Pearson, W.R., Lipman, D.J., 1988. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA 85, 2444-2448.
22. Saito, A., Watanabe, T.K., Shimada, Y., Fujiwara, T., Slaughter, C.A., DeMartino, G.N., Tanahashi, N., Tanaka, K., 1997. cDNA cloning and functional analysis of p44.5 and p55, two regulatory subunits, of the 26S proteasome. Gene 203, 241-250.
23. Sherman, F., 1991. Getting started with yeast. In: Guthrie, C., Fink, G.R. (Eds.) Methods in Enzymology, vol. 194. Guide to Yeast Genetics and Molecular Biology, Academic Press, Inc., New York, pp. 3-21.
24. +-dependent transcription and is implicated in the maintenance of chromosome structure. 1995. J. Cell Sci. 108, 569-579.
25. Spataro, V., Toda, T., Craig, R., Seeger, M., Dubiel, W., Harris, A.L., Norbury, C., 1997. Resistance to diverse drugs and ultraviolet light conferred by overexpression of a novel human 26S proteasome sub-unit. J. Biol. Chem. 272, 30470-30475.
26. Tanaka, K., 1998. Molecular biology of the proteasome. Biochem. Biophys. Res. Commun. 247, 537-541.
27. Tanaka, K., Tsurumi, C., 1997. The 26S proteasome: subunits and functions. Mol. Biol. Rep. 24, 3-11.
28. Thompson, C.C., Brown, T.A., McKnight, S.L., 1991. Convergence of Ets- and notch-related structural motifs in a heteromeric DNA binding complex. Science 253, 762-768.
29. Tsurumi, C., DeMartino, G.N., Slaughter, C.A., Shimbara, N., Tanaka, K., 1995. cDNA cloning of p40, a regulatory subunit of the human 26S proteasome, a homolog of Mov-34 gene product. Biochem. Biophys. Res. Commun. 210, 600-608.
30. Tsurumi, C., Shimizu, Y., Saeki, M., Sato, S., DeMartino, G.N., Slaughter, C.A., Fujimuro, M., Yokosawa, H., Yamasaki, M., Hendil, K.B., Toh-e, A., Tanahashi, N., Tanaka, K., 1996. cDNA cloning and functional analysis of the p97 subunit of the 26S proteasome, a polypeptide identical to the type 1 tumor-necrosis-factor-receptor-associated protein-2/55.11. Eur. J. Biochem. 239, 912-921.
31. van Nocker, S., Sadis, S., Rubin, D.M., Glickman, M., Fu, H., Coux, O., Wefes, I., Finley, D., Vierstra, R.D., 1996. 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. Mol. Cell. Biol. 16, 6020-6028.
32. Wach, A., 1996. PCR-synthesis of marker cassettes with long flanking homology regions for gene disruption in S. cerevisiae. Yeast 12, 259-265.
33. Yokota, K., Kagawa, S., Shimizu, Y., Akioka, H., Tsurumi, C., Noda, C., Fujimuro, M., Yokosawa, H., Fujiwara, T., Takahashi, E., Ohba, M., Yamasaki, M., DeMartino, G.N., Slaughter, C.A., Toh-e, A., Tanaka, K., 1996. cDNA cloning of p112, the largest regulatory subunit of the human 26S proteasome, and functional analysis of its yeast homologue Sen3p. Mol. Biol. Cell 7, 853-870.