Phylogenetic Analyses of Proteins Coordinating G2 Size Control in Fission Yeast

  • Zsófia Nagy Department of Applied Biotechnology and Food Science, Faculty of Chemical Technology and Biotechnology, Budapest University of Technology and Economics, H-1521 Budapest, P.O.B. 91, Hungary
  • Anna Medgyes-Horváth Department of Applied Biotechnology and Food Science, Faculty of Chemical Technology and Biotechnology, Budapest University of Technology and Economics, H-1521 Budapest, P.O.B. 91, Hungary; Department of Physics of Complex Systems, Institute of Physics, Faculty of Science, Eötvös Loránd University, H-1518 Budapest, P.O.B. 32, Hungary
  • Csilla Szalay Department of Applied Biotechnology and Food Science, Faculty of Chemical Technology and Biotechnology, Budapest University of Technology and Economics, H-1521 Budapest, P.O.B. 91, Hungary
  • Matthias Sipiczki Department of Genetics and Applied Microbiology, Faculty of Science and Technology, University of Decrecen, H-4002 Debrecen, P.O.B. 400, Hungary
  • Ákos Sveiczer Department of Applied Biotechnology and Food Science, Faculty of Chemical Technology and Biotechnology, Budapest University of Technology and Economics, H-1521 Budapest, P.O.B. 91, Hungary

Abstract

Regulation of G2 phase is based on inhibition of MPF (M-phase Promoting Factor) through phosphorylation by Wee1-like kinases. Removal of the inhibiting phosphate group requires Cdc25-like phosphatases. In fission yeast, size control is achieved by monitoring cell length via interactions of Pom1, Nif1, Cdr1 and Cdr2 proteins, regulating MPF via the Wee1 kinase. Here, a search for homologues of these key proteins was performed in the genomes of several model organisms to analyze the evolution of G2 size control. Both the known upstream pathways regulating Wee1 protein (Pom1 → Cdr2, and Nif1 → Cdr1) have been found to be characteristic only in fission yeasts. Mik1, a backup copy of Wee1 kinase probably appeared in the common ancestor of the fission yeasts. The duplication resulting in Wee1A and Wee1B isoforms probably happened in a common ancestor of higher animals, while the Myt1 protein (found only in animals) could be a variant between an ancient serine / threonine kinase and the Wee1 tyrosine kinase. Probably both the ancestors of plants and that of fungi may have lost the myt1 gene. In fission yeasts, Pyp3 is a backup phosphatase of Cdc25, also activating MPF in late G2. Interestingly, we found that the small Ibp1 phosphatase appeared to be a closer homologue of Cdc25, although its function is different. Moreover, Cdc25 homologues identified in plants were found to be more closely related to Ibp1 rather than to Cdc25 of fission yeast. In the Cdc25-like proteins, a novel conserved region was found with the consensus sequence LxxG(Y/F).

Keywords: G2 size control, phylogenetic analysis, fission yeast, Wee1, Cdc25
Published online
2019-07-05
How to Cite
Nagy, Z., Medgyes-Horváth, A., Szalay, C., Sipiczki, M. and Sveiczer, Ákos (2019) “Phylogenetic Analyses of Proteins Coordinating G2 Size Control in Fission Yeast”, Periodica Polytechnica Chemical Engineering, 63(4), pp. 555-568. doi: https://doi.org/10.3311/PPch.14051.
Section
Articles