Identification of partners of TIF34, a component of the yeast eIF3 complex, required for cell proliferation and translation initiation

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...

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Bibliographic Details
Published in:The EMBO journal 1997-11, Vol.16 (22), p.6812-6822
Main Authors: Verlhac, Marie-Hélène, Chen, Ruey-Hwa, Hanachi, Parisa, Hershey, John W.B., Derynck, Rik
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacterial Proteins - metabolism
Base Sequence
Cell Cycle
Cellular Biology
eIF3
Eukaryotic Initiation Factor-3
Fungal Proteins - metabolism
Life Sciences
Mating Factor
Molecular Sequence Data
Mutation
Peptide Initiation Factors - metabolism
Peptides
Protein Binding
Protein Biosynthesis
Repetitive Sequences, Nucleic Acid
Reproduction
Saccharomyces cerevisiae - cytology
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae Proteins
Transcription Factors - genetics
Transcription Factors - metabolism
translation
WD-40 repeats
yeast
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Summary: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.
ISSN:0261-4189
1460-2075
1460-2075
DOI:10.1093/emboj/16.22.6812