title: Evolution and function of the Mycoplasma hyopneumoniae peroxiredoxin, a 2-Cys-like enzyme with a single Cys residue.
abstract: The minimal genome of the mollicute Mycoplasma hyopneumoniae, the etiological agent of porcine enzootic pneumonia, encodes a limited repertoire of antioxidant enzymes that include a single and atypical peroxiredoxin (MhPrx), whose evolution and function were studied here. MhPrx has only one catalytic cysteine, in contrast with some of its possible ancestors (2-Cys peroxiredoxins), which have two. Although it is more similar to 2-Cys orthologs, MhPrx can still function with a single peroxidatic cysteine (CysP), using non-thiolic electron donors to reduce it. Therefore, MhPrx could be a representative of a possible group of 2-Cys peroxiredoxins, which have lost the resolving cysteine (CysR) residue without losing their catalytic properties. To further investigate MhPrx evolution, we performed a comprehensive phylogenetic analysis in the context of several bacterial families, including Prxs belonging to Tpx and AhpE families, shedding light on the evolutionary history of Mycoplasmataceae Prxs and giving support to the hypothesis of a relatively recent loss of the CysRwithin this family. Moreover, mutational analyses provided insights into MhPrx function with one, two, or without catalytic cysteines. While removal of the MhPrx putative CysPcaused complete activity loss, confirming its catalytic role, the introduction of a second cysteine in a site correspondent to that of the CysRof a 2-Cys orthologue, as in the MhPrx supposed ancestral form, was compatible with enzyme activity. Overall, our phylogenetic and mutational studies support that MhPrx recently diverged from a 2-Cys Prx ancestor and pave the way for future studies addressing structural, functional, and evolutive aspects of peroxiredoxin subfamilies in Mollicutes and other bacteria.
authors.affiliation: Laboratório de Genômica Estrutural e Funcional, Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul (UFRGS), Caixa Postal 15005, Porto Alegre, RS, 91501-970, Brazil.|Grupo de Pesquisa em Plasticidade Neuroglial, Departamento de Bioquímica, UFRGS, Porto Alegre, RS, Brazil.
authors.forename: Taylor
authors.initials: T
authors.lastname: Gonchoroski
authors.affiliation: Laboratório de Genômica Estrutural e Funcional, Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul (UFRGS), Caixa Postal 15005, Porto Alegre, RS, 91501-970, Brazil.
authors.forename: Veridiana G
authors.initials: VG
authors.lastname: Virginio
authors.affiliation: Unidade de Biologia Teórica e Computacional, Centro de Biotecnologia, UFRGS, Porto Alegre, RS, Brazil.
authors.forename: Claudia E
authors.initials: CE
authors.lastname: Thompson
authors.affiliation: Laboratório de Genômica Estrutural e Funcional, Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul (UFRGS), Caixa Postal 15005, Porto Alegre, RS, 91501-970, Brazil.|Programa de Pós-Graduação em Biologia Celular e Molecular, Centro de Biotecnologia, UFRGS, Porto Alegre, RS, Brazil.
authors.forename: Jéssica A
authors.initials: JA
authors.lastname: Paes
authors.affiliation: Laboratório de Genômica Estrutural e Funcional, Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul (UFRGS), Caixa Postal 15005, Porto Alegre, RS, 91501-970, Brazil.|Programa de Pós-Graduação em Biologia Celular e Molecular, Centro de Biotecnologia, UFRGS, Porto Alegre, RS, Brazil.|Departamento de Criminalística, Instituto Geral de Perícias do Rio Grande do Sul, Porto Alegre, RS, Brazil.
authors.forename: Cláudio X
authors.initials: CX
authors.lastname: Machado
authors.affiliation: Laboratório de Genômica Estrutural e Funcional, Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul (UFRGS), Caixa Postal 15005, Porto Alegre, RS, 91501-970, Brazil. henrique@cbiot.ufrgs.br.|Programa de Pós-Graduação em Biologia Celular e Molecular, Centro de Biotecnologia, UFRGS, Porto Alegre, RS, Brazil. henrique@cbiot.ufrgs.br.|Departamento de Biologia Molecular e Biotecnologia, Instituto de Biociências, UFRGS, Porto Alegre, RS, Brazil. henrique@cbiot.ufrgs.br.
authors.forename: Henrique B
authors.initials: HB
authors.lastname: Ferreira
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism; D002384:Catalysis; D003001:Cloning, Molecular; D003545:Cysteine / Q000235:genetics*; D004252:DNA Mutational Analysis; D004583:Electrons; D019143:Evolution, Molecular; D016680:Genome, Bacterial; D008670:Metals / Q000737:chemistry; D016297:Mutagenesis, Site-Directed; D045705:Mycoplasma hyopneumoniae / Q000201:enzymology* / Q000235:genetics; D010100:Oxygen / Q000737:chemistry; D010544:Peroxidases / Q000378:metabolism; D054464:Peroxiredoxins / Q000235:genetics* / Q000378:metabolism; D010802:Phylogeny; D011994:Recombinant Proteins / Q000235:genetics; D013438:Sulfhydryl Compounds / Q000737:chemistry
chemical_list: D001426:Bacterial Proteins; D008670:Metals; D011994:Recombinant Proteins; D013438:Sulfhydryl Compounds; D010544:Peroxidases; D054464:Peroxiredoxins; D003545:Cysteine; D010100:Oxygen
keywords: AhpE; Molecular evolution; Mycoplasma; Peroxiredoxin; Tpx