ArticleThe EMBO journal1997
Identification of partners of TIF34, a component of the yeast eIF3 complex, required for cell proliferation and translation initiation.
Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 56 citations in OpenAlex.
- eIF3: a critical player in mRNA recruitment to the ribosome with emerging roles across translation.Biochemical Society transactions · 2025Review
- Engineered transient and stable overexpression of translation factors eIF3i and eIF3c in CHOK1 and HEK293 cells gives enhanced cell growth associated with increased c-Myc expression and increased recombinant protein synthesis.Metabolic engineering · 2020Article
- The translational factor eIF3f: the ambivalent eIF3 subunit.Cellular and molecular life sciences : CMLS · 2013Review
- Article
- 'Ribozoomin'--translation initiation from the perspective of the ribosome-bound eukaryotic initiation factors (eIFs).Current protein & peptide science · 2012Review
- Functional reconstitution of human eukaryotic translation initiation factor 3 (eIF3).Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- A protein network-guided screen for cell cycle regulators in Drosophila.BMC systems biology · 2011Article
- Distinct regions of human eIF3 are sufficient for binding to the HCV IRES and the 40S ribosomal subunit.Journal of molecular biology · 2010Article
- Power of yeast for analysis of eukaryotic translation initiation.The Journal of biological chemistry · 2010Review
- The RNA recognition motif of eukaryotic translation initiation factor 3g (eIF3g) is required for resumption of scanning of posttermination ribosomes for reinitiation on GCN4 and together with eIF3i stimulates linear scanning.Molecular and cellular biology · 2010Article
- A quantitative estimation of the global translational activity in logarithmically growing yeast cells.BMC systems biology · 2008Article
- Reconstitution reveals the functional core of mammalian eIF3.The EMBO journal · 2007Article
- Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e subunit.The Journal of biological chemistry · 2006Article
- Eucaryotic initiation factor 4B controls eIF3-mediated ribosomal entry of viral reinitiation factor.The EMBO journal · 2004Article
- Rootstock effects on gene expression patterns in apple tree scions.Plant molecular biology · 2003Article
- The yeast eIF3 subunits TIF32/a, NIP1/c, and eIF5 make critical connections with the 40S ribosome in vivo.Genes & development · 2003Article
- Sum1, a component of the fission yeast eIF3 translation initiation complex, is rapidly relocalized during environmental stress and interacts with components of the 26S proteasome.Molecular biology of the cell · 2002Article
- Induction of a mitosis delay and cell lysis by high-level secretion of mouse alpha-amylase from Saccharomyces cerevisiae.Applied and environmental microbiology · 2001Article
- Conserved bipartite motifs in yeast eIF5 and eIF2Bepsilon, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2.The EMBO journal · 1999Article
- Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5.Molecular and cellular biology · 1998Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Eukaryotic initiation factor-3 (eIF3) in the yeast Saccharomyces cerevisiae plays a central role in initiation of translation. The eIF3 complex contains at least eight different proteins, but, as yet, little is known about the function of the individual proteins. In this study we have characterized the role of TIF34 (eIF3-p39), a recently identified WD-40 domain-containing protein of 39 kDa, in the eIF3 complex. Using temperature-sensitive mutants of TIF34 we show that this protein is required for cell cycle progression and for mating and plays an essential role in initiation of protein synthesis. By two-hybrid screening we have identified two partners that directly associate with TIF34: PRT1, a previously characterized eIF3 subunit, and a novel protein of 33 kDa (eIF3-p33) which is part of the eIF3 complex and has an RNA binding domain. TIF34 and p33 interact with each other and overexpression of p33 complements the growth defect of a tif34-ts mutant. Our results provide support for both physical and functional interactions between three subunits, TIF34, PRT1 and p33, in the eIF3 complex.
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