eIF4Es and Their Interactors from Yeast Species

Ross, Daniela; Altmann, Michael (2016). eIF4Es and Their Interactors from Yeast Species. In: Hernández, Greco; Jagus, Rosemary (eds.) Evolution of The Protein Synthesis Machinery and Its Regulation (pp. 143-164). Sprinter International 10.1007/978-3-319-39468-8_7

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The kingdom Fungi is divided into six phyla, namely Microspora, Zygomycota,
Glomeromycota, Ascomycota, Basidiomycota and Lichens (see Fig. 1a). Phylum
Ascomycota is divided into the subphyla Taphrinomycotina, Saccharomycotina and Pezizomycotina [1]. In this chapter we describe the variety of eIF4Es and associated proteins in unicellular fungi belonging to the subphyla Taphrinomycotina and Saccharomycotina, which are generally quoted as yeasts. The third subphylum, Pezizomycotina (consisting mostly of mould species such as Penicillium and Aspergillus), is not clearly defined as uni- or multicellular and will not be further analysed in this chapter. The best known yeast species are Saccharomyces cerevisiae (budding yeast) and
Schizosaccharomyces pombe (fission yeast). Both species belong to the subphyla Saccharomycotina/“true yeasts” and Taphrinomycotina, respectively (for more details on phylogenetic classification data, see Fig. 1b). Though unicellular, yeast populations possess—especially when under stress—multicellular-like properties such as pseudohyphenation [2, 3] and quorum sensing, thereby increasing their survival potential [4].
The genomes of baker’s budding yeast Saccharomyces cerevisiae and fission
yeast Schizosaccharomyces pombe were sequenced about 15–20 years ago and, as versatile model organisms, have rendered plenty of biological information to our current knowledge on eukaryotic processes. The genomic sequencing of less known unicellular yeast species has been pursued in recent years, thereby allowing comparative studies of all gene encoding translation factors. In this chapter, we will review the current knowledge on the following initiation factors from yeasts: thecap-binding protein eIF4E and its interactor eIF4G, which acts as a scaffold Protein for further initiation factors (eIF4E and eIF4G form together with the helicase eIF4A the eIF4F complex), as well as two further eIF4E interactors termed p20 and Eap1 that we will discuss in this study. We also will comment on the evolutionary implications of the new findings mentioned here.

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