Potential role of acetyl-CoA synthetase (acs) and malate dehydrogenase (mae) in the evolution of the acetate switch in Bacteria and Archaea

Elliott P. Barnhart; Marcella A. McClure; Kiki Johnson; Sean Cleveland; Kristopher A. Hunt; Matthew W. Fields

doi:10.1038/srep12498

Potential role of acetyl-CoA synthetase (acs) and malate dehydrogenase (mae) in the evolution of the acetate switch in Bacteria and Archaea

Scientific Reports

By: Elliott P. Barnhart, Marcella A. McClure, Kiki Johnson, Sean Cleveland, Kristopher A. Hunt, and Matthew W. Fields

https://doi.org/10.1038/srep12498

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Abstract

Although many Archaea have AMP-Acs (acetyl-coenzyme A synthetase) and ADP-Acs, the extant methanogenic genus Methanosarcina is the only identified Archaeal genus that can utilize acetate via acetate kinase (Ack) and phosphotransacetylase (Pta). Despite the importance of ack as the potential urkinase in the ASKHA phosphotransferase superfamily, an origin hypothesis does not exist for the acetate kinase in Bacteria, Archaea, or Eukarya. Here we demonstrate that Archaeal AMP-Acs and ADP-Acs contain paralogous ATPase motifs previously identified in Ack, which demonstrate a novel relation between these proteins in Archaea. The identification of ATPase motif conservation and resulting structural features in AMP- and ADP-acetyl-CoA synthetase proteins in this study expand the ASKHA superfamily to include acetyl-CoA synthetase. Additional phylogenetic analysis showed that Pta and MaeB sequences had a common ancestor, and that the Pta lineage within the halophilc archaea was an ancestral lineage. These results suggested that divergence of a duplicated maeB within an ancient halophilic, archaeal lineage formed a putative pta ancestor. These results provide a potential scenario for the establishment of the Ack/Pta pathway and provide novel insight into the evolution of acetate metabolism for all three domains of life.

Additional publication details
Publication type	Article
Publication Subtype	Journal Article
Title	Potential role of acetyl-CoA synthetase (acs) and malate dehydrogenase (mae) in the evolution of the acetate switch in Bacteria and Archaea
Series title	Scientific Reports
DOI	10.1038/srep12498
Volume	5
Year Published	2015
Language	English
Publisher	Nature
Contributing office(s)	WY-MT Water Science Center
Description	Article number: 12498; 10 p.
First page	1
Last page	10
Google Analytic Metrics	Metrics page