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: , and 

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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