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. 2016 Mar 4;291(10):5199-205.
doi: 10.1074/jbc.M115.691428. Epub 2016 Jan 7.

Evolutionary Ancestry of Eukaryotic Protein Kinases and Choline Kinases

Affiliations

Evolutionary Ancestry of Eukaryotic Protein Kinases and Choline Kinases

Shenshen Lai et al. J Biol Chem. .

Abstract

The reversible phosphorylation of proteins catalyzed by protein kinases in eukaryotes supports an important role for eukaryotic protein kinases (ePKs) in the emergence of nucleated cells in the third superkingdom of life. Choline kinases (ChKs) could also be critical in the early evolution of eukaryotes, because of their function in the biosynthesis of phosphatidylcholine, which is unique to eukaryotic membranes. However, the genomic origins of ePKs and ChKs are unclear. The high degeneracy of protein sequences and broad expansion of ePK families have made this fundamental question difficult to answer. In this study, we identified two class-I aminoacyl-tRNA synthetases with high similarities to consensus amino acid sequences of human protein-serine/threonine kinases. Comparisons of primary and tertiary structures supported that ePKs and ChKs evolved from a common ancestor related to glutaminyl aminoacyl-tRNA synthetases, which may have been one of the key factors in the successful of emergence of ancient eukaryotic cells from bacterial colonies.

Keywords: aminoacyl tRNA synthetase; choline kinase; glutaminyl aminoacyl tRNA synthetase; phosphatidylcholine biosynthesis; protein evolution; protein kinase; protein phosphorylation; signal transduction.

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Figures

FIGURE 1.
FIGURE 1.
Structural comparisons of protein-serine/threonine kinases, choline kinases, and glutaminyl-tRNA synthetases. The identity and similarity of each pair (gray text) were calculated based on primary amino acid consensus sequences. The Protein Data Bank (PDB) IDs of each three-dimensional (3D) structure used for comparison are shown in dark circles and linked with scores generated from the RCSB PDB Protein Comparison Tool.
FIGURE 2.
FIGURE 2.
Comparison of three-dimensional structures of protein-serine/threonine kinases, choline kinase, and glutaminyl tRNA synthetase. A, glutaminyl-tRNA synthetase (PDB ID: 4R3Z chain C, red) with choline kinase (PDB ID: 2IG7, blue). B, glutaminyl-tRNA synthetase (PDB ID: 4R3Z chain C, red) with microtubule affinity-regulating kinase (PDB ID: 2R0I, blue). C, PKA (PDB ID: 3DND, red) with choline/ethanolamine kinase (PDB ID: 2IG7, blue). All sequences were from human proteins. The comparisons were done by RCSB PDB Protein Comparison Tool using the jFatCat Java Web Start (rigid) method. Two different angles of each alignment are shown.

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