Literature DB >> 29138003

Serine/Threonine Protein Kinases from Bacteria, Archaea and Eukarya Share a Common Evolutionary Origin Deeply Rooted in the Tree of Life.

Ivan Andreas Stancik1, Martin Sebastijan Šestak2, Boyang Ji3, Marina Axelson-Fisk4, Damjan Franjevic5, Carsten Jers6, Tomislav Domazet-Lošo7, Ivan Mijakovic8.   

Abstract

The main family of serine/threonine/tyrosine protein kinases present in eukarya was defined and described by Hanks et al. in 1988 (Science, 241, 42-52). It was initially believed that these kinases do not exist in bacteria, but extensive genome sequencing revealed their existence in many bacteria. For historical reasons, the term "eukaryotic-type kinases" propagated in the literature to describe bacterial members of this protein family. Here, we argue that this term should be abandoned as a misnomer, and we provide several lines of evidence to support this claim. Our comprehensive phylostratigraphic analysis suggests that Hanks-type kinases present in eukarya, bacteria and archaea all share a common evolutionary origin in the lineage leading to the last universal common ancestor (LUCA). We found no evidence to suggest substantial horizontal transfer of genes encoding Hanks-type kinases from eukarya to bacteria. Moreover, our systematic structural comparison suggests that bacterial Hanks-type kinases resemble their eukaryal counterparts very closely, while their structures appear to be dissimilar from other kinase families of bacterial origin. This indicates that a convergent evolution scenario, by which bacterial kinases could have evolved a kinase domain similar to that of eukaryal Hanks-type kinases, is not very likely. Overall, our results strongly support a monophyletic origin of all Hanks-type kinases, and we therefore propose that this term should be adopted as a universal name for this protein family.
Copyright © 2017 The Author(s). Published by Elsevier Ltd.. All rights reserved.

Keywords:  Hanks-type kinase; bacterial protein kinase; eSTK; eukaryotic-type kinase; phylostratigraphy

Mesh:

Substances:

Year:  2017        PMID: 29138003     DOI: 10.1016/j.jmb.2017.11.004

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  22 in total

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4.  The biology of thermoacidophilic archaea from the order Sulfolobales.

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7.  Dual regulation of activity and intracellular localization of the PASTA kinase PrkC during Bacillus subtilis growth.

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8.  Phosphorylation of the Bacillus subtilis Replication Controller YabA Plays a Role in Regulation of Sporulation and Biofilm Formation.

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Review 9.  Regulation of Protein Post-Translational Modifications on Metabolism of Actinomycetes.

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Review 10.  Hanks-Type Serine/Threonine Protein Kinases and Phosphatases in Bacteria: Roles in Signaling and Adaptation to Various Environments.

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