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dc.contributor.authorBarnhart, Elliott P.
dc.contributor.authorMcClure, Marcella A.
dc.contributor.authorJohnson, Kiki
dc.contributor.authorCleveland, Sean
dc.contributor.authorHunt, Kristopher A.
dc.contributor.authorFields, Matthew W.
dc.date.accessioned2015-12-07T17:41:44Z
dc.date.available2015-12-07T17:41:44Z
dc.date.issued2015-08
dc.identifier.citationBarnhart, Elliott P., Marcella A. McClure, Kiki Johnson, Sean Cleveland, Kristopher A. Hunt, and Matthew W. Fields. "Potential Role of Acetyl-CoA Synthetase (acs) & Malate Dehydrogenase (mae) in the Evolution of the Acetate Switch in Bacteria and Archaea." Scientific Reports 5 (August 2015): 12498. DOI:https://dx.doi.org/10.1038/srep12498 .en_US
dc.identifier.issn2045-2322
dc.identifier.urihttps://scholarworks.montana.edu/xmlui/handle/1/9398
dc.description.abstractAlthough 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.en_US
dc.description.sponsorshipDE-AC02-05CH11231; DOE-ZERT Program under grant No. DE-FC26-04NT42262.en_US
dc.rightsCC BY 4.0en_US
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/legalcodeen_US
dc.titlePotential Role of Acetyl-CoA Synthetase (acs) & Malate Dehydrogenase (mae) in the Evolution of the Acetate Switch in Bacteria and Archaeaen_US
dc.typeArticleen_US
mus.citation.extentfirstpage12498en_US
mus.citation.extentlastpage12498en_US
mus.citation.journaltitleScientific Reportsen_US
mus.citation.volume5en_US
mus.identifier.categoryEngineering & Computer Scienceen_US
mus.identifier.categoryLife Sciences & Earth Sciencesen_US
mus.identifier.doi10.1038/srep12498en_US
mus.relation.collegeCollege of Agricultureen_US
mus.relation.collegeCollege of Engineeringen_US
mus.relation.departmentCenter for Biofilm Engineering.en_US
mus.relation.departmentMicrobiology & Immunology.en_US
mus.relation.universityMontana State University - Bozemanen_US
mus.data.thumbpage3en_US
mus.contributor.orcidFields, Matthew W.|0000-0001-9053-1849en_US


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