Nin1p, a regulatory subunit of the 26S proteasome, is necessary for activation of Cdc28p kinase of Saccharomyces cerevisiae

K. Kominami -i., G. N. DeMartino, C. R. Moomaw, Clive A. Slaughter, N. Shimbara, M. Fujimuro, H. Yokosawa, H. Hisamatsu, N. Tanahashi, Y. Shimizu, K. Tanaka, A. Toh-e

Research output: Contribution to journalArticle

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Abstract

The nin1-1 mutant of Saccharomyces cerevisiae cannot perform the G1/S and G2/M transitions at restrictive temperatures. At such temperatures, nin1-1 strains fail to activate histone H1 kinase after release from alpha factor-imposed G1 block and after release from hydroxyurea-imposed S block. The nin1-1 mutation shows synthetic lethality with certain cdc28 mutant alleles such as cdc28-1N. Two lines of evidence indicate that Nin1p is a component of the 26S proteasome complex: (i) Nin1p, as well as the known component of the 26S proteasome, shifted to the 26S proteasome peak in the glycerol density gradient after preincubation of crude extract with ATP-Mg2+, and (ii) nin1-1 cells accumulated polyubiquitinated proteins under restrictive conditions. These results suggest that activation of Cdc28p kinase requires proteolysis. We have cloned a human cDNA encoding a regulatory subunit of the 26S proteasome, p31, which was found to be a homolog of Nin1p.

Original languageEnglish (US)
Pages (from-to)3105-3115
Number of pages11
JournalEMBO Journal
Volume14
Issue number13
StatePublished - Jan 1 1995
Externally publishedYes

Fingerprint

Yeast
Saccharomyces cerevisiae
Phosphotransferases
Chemical activation
Proteolysis
Temperature
Hydroxyurea
Complex Mixtures
Glycerol
Complementary DNA
Adenosine Triphosphate
Alleles
Mutation
ATP dependent 26S protease
Proteins

Keywords

  • 26S proteasome
  • Cdc28p kinase
  • Cell cycle
  • NIN1
  • Saccharomyces cerevisiae

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

Cite this

Kominami -i., K., DeMartino, G. N., Moomaw, C. R., Slaughter, C. A., Shimbara, N., Fujimuro, M., ... Toh-e, A. (1995). Nin1p, a regulatory subunit of the 26S proteasome, is necessary for activation of Cdc28p kinase of Saccharomyces cerevisiae. EMBO Journal, 14(13), 3105-3115.

Nin1p, a regulatory subunit of the 26S proteasome, is necessary for activation of Cdc28p kinase of Saccharomyces cerevisiae. / Kominami -i., K.; DeMartino, G. N.; Moomaw, C. R.; Slaughter, Clive A.; Shimbara, N.; Fujimuro, M.; Yokosawa, H.; Hisamatsu, H.; Tanahashi, N.; Shimizu, Y.; Tanaka, K.; Toh-e, A.

In: EMBO Journal, Vol. 14, No. 13, 01.01.1995, p. 3105-3115.

Research output: Contribution to journalArticle

Kominami -i., K, DeMartino, GN, Moomaw, CR, Slaughter, CA, 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 Journal, vol. 14, no. 13, pp. 3105-3115.
Kominami -i. K, DeMartino GN, Moomaw CR, Slaughter CA, Shimbara N, Fujimuro M et al. Nin1p, a regulatory subunit of the 26S proteasome, is necessary for activation of Cdc28p kinase of Saccharomyces cerevisiae. EMBO Journal. 1995 Jan 1;14(13):3105-3115.
Kominami -i., K. ; DeMartino, G. N. ; Moomaw, C. R. ; Slaughter, Clive A. ; Shimbara, N. ; Fujimuro, M. ; Yokosawa, H. ; Hisamatsu, H. ; Tanahashi, N. ; Shimizu, Y. ; Tanaka, K. ; Toh-e, A. / Nin1p, a regulatory subunit of the 26S proteasome, is necessary for activation of Cdc28p kinase of Saccharomyces cerevisiae. In: EMBO Journal. 1995 ; Vol. 14, No. 13. pp. 3105-3115.
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abstract = "The nin1-1 mutant of Saccharomyces cerevisiae cannot perform the G1/S and G2/M transitions at restrictive temperatures. At such temperatures, nin1-1 strains fail to activate histone H1 kinase after release from alpha factor-imposed G1 block and after release from hydroxyurea-imposed S block. The nin1-1 mutation shows synthetic lethality with certain cdc28 mutant alleles such as cdc28-1N. Two lines of evidence indicate that Nin1p is a component of the 26S proteasome complex: (i) Nin1p, as well as the known component of the 26S proteasome, shifted to the 26S proteasome peak in the glycerol density gradient after preincubation of crude extract with ATP-Mg2+, and (ii) nin1-1 cells accumulated polyubiquitinated proteins under restrictive conditions. These results suggest that activation of Cdc28p kinase requires proteolysis. We have cloned a human cDNA encoding a regulatory subunit of the 26S proteasome, p31, which was found to be a homolog of Nin1p.",
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AU - Moomaw, C. R.

AU - Slaughter, Clive A.

AU - Shimbara, N.

AU - Fujimuro, M.

AU - Yokosawa, H.

AU - Hisamatsu, H.

AU - Tanahashi, N.

AU - Shimizu, Y.

AU - Tanaka, K.

AU - Toh-e, A.

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