Yeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multicopy suppressors of nin1-1

Kin Ichiro Kominami, Naganari Okura, Motohiro Kawamura, George N. DeMartino, Clive A. Slaughter, Naoki Shimbara, Chin Ha Chung, Masahiro Fujimuro, Hideyoshi Yokosawa, Yoshihisa Shimizu, Nobuyuki Tanahashi, Keiji Tanaka, Akio Toh-e

Research output: Contribution to journalArticle

87 Citations (Scopus)

Abstract

Nin1p, a component of the 26S proteasome of Saccharomyces cerevisiae, is required for activation of Cdc28p kinase at the G1-S-phase and G2-M boundaries. By exploiting the temperature-sensitive phenotype of the nin1-1 mutant, we have screened for genes encoding proteins with related functions to Nin1p and have cloned and characterized two new multicopy suppressors, SUN1 and SUN2, of the nin1-1 mutation. SUN1 can suppress a null nin1 mutation, whereas SUN2, an essential gene, does not. Sun1p is a 268-amino acid protein which shows strong similarity to MBP1 of Arabidopsis thaliana, a homologue of the S5a subunit of the human 26S proteasome. Sun1p binds ubiquitin-lysozyme conjugates as do S5a and MBP1. Sun2p (523 amino acids) was found to be homologous to the p58 subunit of the human 26S proteasome. cDNA encoding the p58 component was cloned. Furthermore, expression of a derivative of p58 from which the N-terminal 150 amino acids had been removed restored the function of a null allele of SUN2. During glycerol density gradient centrifugation, both Sun1p and Sun2p comigrated with the known proteasome components. These results, as well as other structural and functional studies, indicate that both Sun1p and Sun2p are components of the regulatory module of the yeast 26S proteasome.

Original languageEnglish (US)
Pages (from-to)171-187
Number of pages17
JournalMolecular Biology of the Cell
Volume8
Issue number1
DOIs
StatePublished - Jan 1 1997
Externally publishedYes

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Yeasts
Amino Acids
Mutation
Density Gradient Centrifugation
Essential Genes
G1 Phase
Proteasome Endopeptidase Complex
Muramidase
Ubiquitin
S Phase
Arabidopsis
Glycerol
Saccharomyces cerevisiae
Proteins
Phosphotransferases
Complementary DNA
Alleles
Phenotype
Temperature
ATP dependent 26S protease

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

Yeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multicopy suppressors of nin1-1. / Kominami, Kin Ichiro; Okura, Naganari; Kawamura, Motohiro; DeMartino, George N.; Slaughter, Clive A.; Shimbara, Naoki; Chung, Chin Ha; Fujimuro, Masahiro; Yokosawa, Hideyoshi; Shimizu, Yoshihisa; Tanahashi, Nobuyuki; Tanaka, Keiji; Toh-e, Akio.

In: Molecular Biology of the Cell, Vol. 8, No. 1, 01.01.1997, p. 171-187.

Research output: Contribution to journalArticle

Kominami, KI, Okura, N, Kawamura, M, DeMartino, GN, Slaughter, CA, Shimbara, N, Chung, CH, 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 suppressors of nin1-1', Molecular Biology of the Cell, vol. 8, no. 1, pp. 171-187. https://doi.org/10.1091/mbc.8.1.171
Kominami, Kin Ichiro ; Okura, Naganari ; Kawamura, Motohiro ; DeMartino, George N. ; Slaughter, Clive A. ; Shimbara, Naoki ; Chung, Chin Ha ; Fujimuro, Masahiro ; Yokosawa, Hideyoshi ; Shimizu, Yoshihisa ; Tanahashi, Nobuyuki ; Tanaka, Keiji ; Toh-e, Akio. / Yeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multicopy suppressors of nin1-1. In: Molecular Biology of the Cell. 1997 ; Vol. 8, No. 1. pp. 171-187.
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abstract = "Nin1p, a component of the 26S proteasome of Saccharomyces cerevisiae, is required for activation of Cdc28p kinase at the G1-S-phase and G2-M boundaries. By exploiting the temperature-sensitive phenotype of the nin1-1 mutant, we have screened for genes encoding proteins with related functions to Nin1p and have cloned and characterized two new multicopy suppressors, SUN1 and SUN2, of the nin1-1 mutation. SUN1 can suppress a null nin1 mutation, whereas SUN2, an essential gene, does not. Sun1p is a 268-amino acid protein which shows strong similarity to MBP1 of Arabidopsis thaliana, a homologue of the S5a subunit of the human 26S proteasome. Sun1p binds ubiquitin-lysozyme conjugates as do S5a and MBP1. Sun2p (523 amino acids) was found to be homologous to the p58 subunit of the human 26S proteasome. cDNA encoding the p58 component was cloned. Furthermore, expression of a derivative of p58 from which the N-terminal 150 amino acids had been removed restored the function of a null allele of SUN2. During glycerol density gradient centrifugation, both Sun1p and Sun2p comigrated with the known proteasome components. These results, as well as other structural and functional studies, indicate that both Sun1p and Sun2p are components of the regulatory module of the yeast 26S proteasome.",
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AU - Fujimuro, Masahiro

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