Evolution of 14-3-3 Proteins in Angiosperm Plants: Recurring Gene Duplication and Loss.

Yulia V Mikhaylova,Maria F Shishova,Roman K Puzanskiy

doi:10.3390/plants10122724

Yulia V Mikhaylova, Maria F Shishova + Show 1 more

Open Access

https://doi.org/10.3390/plants10122724

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Abstract

14-3-3 proteins are key regulatory factors in plants and are involved in a broad range of physiological processes. We addressed the evolutionary history of 14-3-3s from 46 angiosperm species, including basal angiosperm Amborella and major lineage of monocotyledons and eudicotyledons. Orthologs of Arabidopsis isoforms were detected. There were several rounds of duplication events in the evolutionary history of the 14-3-3 protein family in plants. At least four subfamilies (iota, epsilon, kappa, and psi) formed as a result of ancient duplication in a common ancestor of angiosperm plants. Recent duplication events followed by gene loss in plant lineage, among others Brassicaceae, Fabaceae, and Poaceae, further shaped the high diversity of 14-3-3 isoforms in plants. Coexpression data showed that 14-3-3 proteins formed different functional groups in different species. In some species, evolutionarily related groups of 14-3-3 proteins had coexpressed together under certain physiological conditions, whereas in other species, closely related isoforms expressed in the opposite manner. A possible explanation is that gene duplication and loss is accompanied by functional plasticity of 14-3-3 proteins.

Highlights

The 14-3-3 proteins belong to the conservative family of proteins, present in all eukaryotes. 14-3-3s modulate activity of various targets in a cell via protein–protein interaction in phosphorylation-dependent mode [1]
We found in analysed species orthologs of Arabidopsis 14-3-3 proteins subfamilies, and checked whether evolutionarily close isoforms had functional similarity
Eleven Poales species were from the grasses family (Poaceae) and one from Bromeliaceae (Ananas)

Summary

Introduction

The 14-3-3 (or GF14) proteins belong to the conservative family of proteins, present in all eukaryotes. 14-3-3s modulate activity of various targets in a cell via protein–protein interaction in phosphorylation-dependent mode [1]. 14-3-3s modulate activity of various targets in a cell via protein–protein interaction in phosphorylation-dependent mode [1]. The first protein from the family was discovered in a cow brain in 1967 [2]. 14-3-3 family members are involved in regulation of processes such as primary metabolism, cell division, growth and differentiation, light, hormone and stress signalling, as well as plant innate immunity [6,7,8,9,10]. The 14-3-3 proteins interact with each other and form homo- or hetero-dimers [11]. Dimers have two domains for interacting with target proteins, which are assumed to be phosphorylated in most cases at the amino acid residues of serine or threonine [12,13]

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Conclusion