Genome-Wide Assessment of Putative Superoxide Dismutases in Unicellular and Filamentous Cyanobacteria

Detalhes bibliográficos
Autor(a) principal: Prajapati,Rajesh
Data de Publicação: 2019
Outros Autores: Yadav,Shivam, Mitra,Sonali, Rai,Priya, Mishra,Rajeev, Atri,Neelam
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Brazilian Archives of Biology and Technology
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132019000100422
Resumo: Abstract Cyanobacteria are photoautotrophic prokaryotes capable to grow in diverse ecological habitats, originated 2.5-3.5 billion years ago and were first to produce oxygen. Since then superoxide dismutases (SOD) acquired great significance due to their ability to catalyze detoxification of byproducts of oxygenic photosynthesis i.e. superoxide radicals. In the present study, we extracted information regarding SODs from species of sequenced cyanobacteria and investigated their diversity, conservation, domain structure, and evolution. 144 putative SOD homologs were identified. Unlike other protein families (ex. serine-threonine kinases) SODs are present in all cyanobacterial species reflecting their significant role in survival. However, their distribution varies fewer (0.01%-0.09%) found in unicellular marine strains whereas abundant (0.02%-0.07%) in filamentous nitrogen-fixing cyanobacteria. They were classified into three major subfamilies according to their domain structures: Fe/MnSOD, Cu/ZnSOD and NiSOD. Interestingly, they lack additional domains as found in proteins of other families however motifs and invariant amino acids typical in eukaryotic SODs were conserved well in these proteins indicating similar catalytic mechanism as eukaryotic SODs. Phylogenetic relationships correspond well with phylogenies based on 16S rRNA and clustering occurs on the basis of structural characteristics such as domain organization. Gene gain-and-loss is insignificant during SOD evolution as evidenced by the absence of additional domain. This study has not only examined an overall background of sequence-structure-function interactions for the SOD gene family but also revealed variation among SOD distribution based on ecophysiological and morphological characters.
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spelling Genome-Wide Assessment of Putative Superoxide Dismutases in Unicellular and Filamentous CyanobacteriaSuperoxide dismutasesCyanobacteriaComparative genomicsPhylogenyAbstract Cyanobacteria are photoautotrophic prokaryotes capable to grow in diverse ecological habitats, originated 2.5-3.5 billion years ago and were first to produce oxygen. Since then superoxide dismutases (SOD) acquired great significance due to their ability to catalyze detoxification of byproducts of oxygenic photosynthesis i.e. superoxide radicals. In the present study, we extracted information regarding SODs from species of sequenced cyanobacteria and investigated their diversity, conservation, domain structure, and evolution. 144 putative SOD homologs were identified. Unlike other protein families (ex. serine-threonine kinases) SODs are present in all cyanobacterial species reflecting their significant role in survival. However, their distribution varies fewer (0.01%-0.09%) found in unicellular marine strains whereas abundant (0.02%-0.07%) in filamentous nitrogen-fixing cyanobacteria. They were classified into three major subfamilies according to their domain structures: Fe/MnSOD, Cu/ZnSOD and NiSOD. Interestingly, they lack additional domains as found in proteins of other families however motifs and invariant amino acids typical in eukaryotic SODs were conserved well in these proteins indicating similar catalytic mechanism as eukaryotic SODs. Phylogenetic relationships correspond well with phylogenies based on 16S rRNA and clustering occurs on the basis of structural characteristics such as domain organization. Gene gain-and-loss is insignificant during SOD evolution as evidenced by the absence of additional domain. This study has not only examined an overall background of sequence-structure-function interactions for the SOD gene family but also revealed variation among SOD distribution based on ecophysiological and morphological characters.Instituto de Tecnologia do Paraná - Tecpar2019-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132019000100422Brazilian Archives of Biology and Technology v.62 2019reponame:Brazilian Archives of Biology and Technologyinstname:Instituto de Tecnologia do Paraná (Tecpar)instacron:TECPAR10.1590/1678-4324-2019170747info:eu-repo/semantics/openAccessPrajapati,RajeshYadav,ShivamMitra,SonaliRai,PriyaMishra,RajeevAtri,Neelameng2019-12-12T00:00:00Zoai:scielo:S1516-89132019000100422Revistahttps://www.scielo.br/j/babt/https://old.scielo.br/oai/scielo-oai.phpbabt@tecpar.br||babt@tecpar.br1678-43241516-8913opendoar:2019-12-12T00:00Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)false
dc.title.none.fl_str_mv Genome-Wide Assessment of Putative Superoxide Dismutases in Unicellular and Filamentous Cyanobacteria
title Genome-Wide Assessment of Putative Superoxide Dismutases in Unicellular and Filamentous Cyanobacteria
spellingShingle Genome-Wide Assessment of Putative Superoxide Dismutases in Unicellular and Filamentous Cyanobacteria
Prajapati,Rajesh
Superoxide dismutases
Cyanobacteria
Comparative genomics
Phylogeny
title_short Genome-Wide Assessment of Putative Superoxide Dismutases in Unicellular and Filamentous Cyanobacteria
title_full Genome-Wide Assessment of Putative Superoxide Dismutases in Unicellular and Filamentous Cyanobacteria
title_fullStr Genome-Wide Assessment of Putative Superoxide Dismutases in Unicellular and Filamentous Cyanobacteria
title_full_unstemmed Genome-Wide Assessment of Putative Superoxide Dismutases in Unicellular and Filamentous Cyanobacteria
title_sort Genome-Wide Assessment of Putative Superoxide Dismutases in Unicellular and Filamentous Cyanobacteria
author Prajapati,Rajesh
author_facet Prajapati,Rajesh
Yadav,Shivam
Mitra,Sonali
Rai,Priya
Mishra,Rajeev
Atri,Neelam
author_role author
author2 Yadav,Shivam
Mitra,Sonali
Rai,Priya
Mishra,Rajeev
Atri,Neelam
author2_role author
author
author
author
author
dc.contributor.author.fl_str_mv Prajapati,Rajesh
Yadav,Shivam
Mitra,Sonali
Rai,Priya
Mishra,Rajeev
Atri,Neelam
dc.subject.por.fl_str_mv Superoxide dismutases
Cyanobacteria
Comparative genomics
Phylogeny
topic Superoxide dismutases
Cyanobacteria
Comparative genomics
Phylogeny
description Abstract Cyanobacteria are photoautotrophic prokaryotes capable to grow in diverse ecological habitats, originated 2.5-3.5 billion years ago and were first to produce oxygen. Since then superoxide dismutases (SOD) acquired great significance due to their ability to catalyze detoxification of byproducts of oxygenic photosynthesis i.e. superoxide radicals. In the present study, we extracted information regarding SODs from species of sequenced cyanobacteria and investigated their diversity, conservation, domain structure, and evolution. 144 putative SOD homologs were identified. Unlike other protein families (ex. serine-threonine kinases) SODs are present in all cyanobacterial species reflecting their significant role in survival. However, their distribution varies fewer (0.01%-0.09%) found in unicellular marine strains whereas abundant (0.02%-0.07%) in filamentous nitrogen-fixing cyanobacteria. They were classified into three major subfamilies according to their domain structures: Fe/MnSOD, Cu/ZnSOD and NiSOD. Interestingly, they lack additional domains as found in proteins of other families however motifs and invariant amino acids typical in eukaryotic SODs were conserved well in these proteins indicating similar catalytic mechanism as eukaryotic SODs. Phylogenetic relationships correspond well with phylogenies based on 16S rRNA and clustering occurs on the basis of structural characteristics such as domain organization. Gene gain-and-loss is insignificant during SOD evolution as evidenced by the absence of additional domain. This study has not only examined an overall background of sequence-structure-function interactions for the SOD gene family but also revealed variation among SOD distribution based on ecophysiological and morphological characters.
publishDate 2019
dc.date.none.fl_str_mv 2019-01-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132019000100422
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132019000100422
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/1678-4324-2019170747
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Instituto de Tecnologia do Paraná - Tecpar
publisher.none.fl_str_mv Instituto de Tecnologia do Paraná - Tecpar
dc.source.none.fl_str_mv Brazilian Archives of Biology and Technology v.62 2019
reponame:Brazilian Archives of Biology and Technology
instname:Instituto de Tecnologia do Paraná (Tecpar)
instacron:TECPAR
instname_str Instituto de Tecnologia do Paraná (Tecpar)
instacron_str TECPAR
institution TECPAR
reponame_str Brazilian Archives of Biology and Technology
collection Brazilian Archives of Biology and Technology
repository.name.fl_str_mv Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)
repository.mail.fl_str_mv babt@tecpar.br||babt@tecpar.br
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