Fission yeast translation initiation factor 3 subunit eIF3h is not essential for global translation initiation, but deletion of eif3h+ affects spore formation

Anirban Ray, Amitabha Bandyopadhyay, Tomohiro Matsumoto, Haiteng Deng, Umadas Maitra

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

The fission yeast Schizosaccharomyces pombe homologue of the p40/eIF3h subunit of mammalian translation initiation factor eIF3 has been characterized in this study. We show that this protein physically associates with the 40S ribosomal particles as a constituent of the multimeric eIF3 protein complex, which consists of all five known eIF3 core subunits (eIF3a, eIF3b, eIF3c, eIF3g and eIF3i) as well as the five non-core subunits (eIF3d, eIF3e, eIF3f, eIF3h and eIF3m) that constitute an eIF3 holocomplex in fission yeast. However, affinity purification of eIF3 from fission yeast cells expressing TAP-tagged eIF3h suggests the presence of distinct forms of eIF3 that differ in their composition of the non-core subunits. Further characterization of eIF3h shows that strains lacking eif 3h+ (eif3hΔ) are viable and show no gross defects, either in vegetative growth or in the rate of in vivo protein synthesis. Polysome profile analysis shows no apparent defects in translation initiation. Furthermore, deletion of eif 3h+ does not affect the ability of the other eIF3 subunits to remain associated with one another in a tight protein complex similar to the situation in wild-type cells. Additionally, we show that human eIF3h can functionally substitute fission yeast eIF3h in complementing in vivo a genetic deletion of eif 3h+. Interestingly, mutant eif3hΔ cells show several prominent phenotypic properties. They are hypersensitive to caffeine and highly defective in meiosis, producing either no spores or incomplete tetrads with a very high frequency. The implications of these results in relation to the functions of eIF3h in Sz. pombe are discussed.

Original languageEnglish (US)
Pages (from-to)809-823
Number of pages15
JournalYeast
Volume25
Issue number11
DOIs
StatePublished - 2008

Fingerprint

Prokaryotic Initiation Factor-3
Schizosaccharomyces
Spores
Yeast
Proteins
Caffeine
Peptide Initiation Factors
Defects
Polyribosomes
Purification
Meiosis
Cells
Chemical analysis
Growth

Keywords

  • Eukaryotic initiation factor 3h subunit
  • Fission yeast
  • Sporulation
  • Translation initiation

ASJC Scopus subject areas

  • Biochemistry
  • Biotechnology
  • Genetics
  • Bioengineering
  • Applied Microbiology and Biotechnology
  • Medicine(all)

Cite this

Fission yeast translation initiation factor 3 subunit eIF3h is not essential for global translation initiation, but deletion of eif3h+ affects spore formation. / Ray, Anirban; Bandyopadhyay, Amitabha; Matsumoto, Tomohiro; Deng, Haiteng; Maitra, Umadas.

In: Yeast, Vol. 25, No. 11, 2008, p. 809-823.

Research output: Contribution to journalArticle

Ray, Anirban ; Bandyopadhyay, Amitabha ; Matsumoto, Tomohiro ; Deng, Haiteng ; Maitra, Umadas. / Fission yeast translation initiation factor 3 subunit eIF3h is not essential for global translation initiation, but deletion of eif3h+ affects spore formation. In: Yeast. 2008 ; Vol. 25, No. 11. pp. 809-823.
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AB - The fission yeast Schizosaccharomyces pombe homologue of the p40/eIF3h subunit of mammalian translation initiation factor eIF3 has been characterized in this study. We show that this protein physically associates with the 40S ribosomal particles as a constituent of the multimeric eIF3 protein complex, which consists of all five known eIF3 core subunits (eIF3a, eIF3b, eIF3c, eIF3g and eIF3i) as well as the five non-core subunits (eIF3d, eIF3e, eIF3f, eIF3h and eIF3m) that constitute an eIF3 holocomplex in fission yeast. However, affinity purification of eIF3 from fission yeast cells expressing TAP-tagged eIF3h suggests the presence of distinct forms of eIF3 that differ in their composition of the non-core subunits. Further characterization of eIF3h shows that strains lacking eif 3h+ (eif3hΔ) are viable and show no gross defects, either in vegetative growth or in the rate of in vivo protein synthesis. Polysome profile analysis shows no apparent defects in translation initiation. Furthermore, deletion of eif 3h+ does not affect the ability of the other eIF3 subunits to remain associated with one another in a tight protein complex similar to the situation in wild-type cells. Additionally, we show that human eIF3h can functionally substitute fission yeast eIF3h in complementing in vivo a genetic deletion of eif 3h+. Interestingly, mutant eif3hΔ cells show several prominent phenotypic properties. They are hypersensitive to caffeine and highly defective in meiosis, producing either no spores or incomplete tetrads with a very high frequency. The implications of these results in relation to the functions of eIF3h in Sz. pombe are discussed.

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