Evolution of Eukaryal and Archaeal Pseudouridine Synthase Pus10
In archaea, pseudouridine (Ψ) synthase Pus10 modifies uridine (U) to Ψ at positions 54 and 55 of tRNA. In contrast, Pus10 is not found in bacteria, where modifications at those two positions are carried out by TrmA (U54 to m 5 U54) and TruB (U55 to Ψ55). Many eukaryotes have an apparent redundancy;...
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description | In archaea, pseudouridine (Ψ) synthase Pus10 modifies uridine (U) to Ψ at positions 54 and 55 of tRNA. In contrast, Pus10 is not found in bacteria, where modifications at those two positions are carried out by TrmA (U54 to m
5
U54) and TruB (U55 to Ψ55). Many eukaryotes have an apparent redundancy; their genomes contain orthologs of archaeal Pus10 and bacterial TrmA and TruB. Although eukaryal Pus10 genes share a conserved catalytic domain with archaeal Pus10 genes, their biological roles are not clear for the two reasons. First, experimental evidence suggests that human Pus10 participates in apoptosis induced by the tumor necrosis factor-related apoptosis-inducing ligand. Whether the function of human Pus10 is in place or in addition to of Ψ synthesis in tRNA is unknown. Second, Pus10 is found in earlier evolutionary branches of fungi (such as chytrid
Batrachochytrium
) but is absent in all dikaryon fungi surveyed (Ascomycetes and Basidiomycetes). We did a comprehensive analysis of sequenced genomes and found that orthologs of Pus10, TrmA, and TruB were present in all the animals, plants, and protozoa surveyed. This indicates that the common eukaryotic ancestor possesses all the three genes. Next, we examined 116 archaeal and eukaryotic Pus10 protein sequences to find that Pus10 existed as a single copy gene in all the surveyed genomes despite ancestral whole genome duplications had occurred. This indicates a possible deleterious gene dosage effect. Our results suggest that functional redundancy result in gene loss or neofunctionalization in different evolutionary lineages. |
doi_str_mv | 10.1007/s00239-018-9827-y |
format | Article |
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5
U54) and TruB (U55 to Ψ55). Many eukaryotes have an apparent redundancy; their genomes contain orthologs of archaeal Pus10 and bacterial TrmA and TruB. Although eukaryal Pus10 genes share a conserved catalytic domain with archaeal Pus10 genes, their biological roles are not clear for the two reasons. First, experimental evidence suggests that human Pus10 participates in apoptosis induced by the tumor necrosis factor-related apoptosis-inducing ligand. Whether the function of human Pus10 is in place or in addition to of Ψ synthesis in tRNA is unknown. Second, Pus10 is found in earlier evolutionary branches of fungi (such as chytrid
Batrachochytrium
) but is absent in all dikaryon fungi surveyed (Ascomycetes and Basidiomycetes). We did a comprehensive analysis of sequenced genomes and found that orthologs of Pus10, TrmA, and TruB were present in all the animals, plants, and protozoa surveyed. This indicates that the common eukaryotic ancestor possesses all the three genes. Next, we examined 116 archaeal and eukaryotic Pus10 protein sequences to find that Pus10 existed as a single copy gene in all the surveyed genomes despite ancestral whole genome duplications had occurred. This indicates a possible deleterious gene dosage effect. Our results suggest that functional redundancy result in gene loss or neofunctionalization in different evolutionary lineages.</description><identifier>ISSN: 0022-2844</identifier><identifier>EISSN: 1432-1432</identifier><identifier>DOI: 10.1007/s00239-018-9827-y</identifier><identifier>PMID: 29349599</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Animal Genetics and Genomics ; Apoptosis ; Archaea ; Bacteria ; Batrachochytrium ; Biomedical and Life Sciences ; Catalysis ; Cell Biology ; Eukaryotes ; Evolution ; Evolutionary Biology ; Fungi ; Gene dosage ; Gene sequencing ; Genes ; Genomes ; Life Sciences ; Microbiology ; Original Article ; Plant Genetics and Genomics ; Plant Sciences ; Protozoa ; Pseudouridine synthase ; Redundancy ; TRAIL protein ; tRNA ; Uridine</subject><ispartof>Journal of molecular evolution, 2018, Vol.86 (1), p.77-89</ispartof><rights>Springer Science+Business Media, LLC, part of Springer Nature 2018</rights><rights>Journal of Molecular Evolution is a copyright of Springer, (2018). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c536t-8fc00f4a55620697d99fadaf124cc9ef1fe1545bdf0a7ae40443a3b558972433</citedby><cites>FETCH-LOGICAL-c536t-8fc00f4a55620697d99fadaf124cc9ef1fe1545bdf0a7ae40443a3b558972433</cites><orcidid>0000-0003-1888-4652</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00239-018-9827-y$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00239-018-9827-y$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,314,780,784,885,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29349599$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fitzek, Elisabeth</creatorcontrib><creatorcontrib>Joardar, Archi</creatorcontrib><creatorcontrib>Gupta, Ramesh</creatorcontrib><creatorcontrib>Geisler, Matt</creatorcontrib><title>Evolution of Eukaryal and Archaeal Pseudouridine Synthase Pus10</title><title>Journal of molecular evolution</title><addtitle>J Mol Evol</addtitle><addtitle>J Mol Evol</addtitle><description>In archaea, pseudouridine (Ψ) synthase Pus10 modifies uridine (U) to Ψ at positions 54 and 55 of tRNA. In contrast, Pus10 is not found in bacteria, where modifications at those two positions are carried out by TrmA (U54 to m
5
U54) and TruB (U55 to Ψ55). Many eukaryotes have an apparent redundancy; their genomes contain orthologs of archaeal Pus10 and bacterial TrmA and TruB. Although eukaryal Pus10 genes share a conserved catalytic domain with archaeal Pus10 genes, their biological roles are not clear for the two reasons. First, experimental evidence suggests that human Pus10 participates in apoptosis induced by the tumor necrosis factor-related apoptosis-inducing ligand. Whether the function of human Pus10 is in place or in addition to of Ψ synthesis in tRNA is unknown. Second, Pus10 is found in earlier evolutionary branches of fungi (such as chytrid
Batrachochytrium
) but is absent in all dikaryon fungi surveyed (Ascomycetes and Basidiomycetes). We did a comprehensive analysis of sequenced genomes and found that orthologs of Pus10, TrmA, and TruB were present in all the animals, plants, and protozoa surveyed. This indicates that the common eukaryotic ancestor possesses all the three genes. Next, we examined 116 archaeal and eukaryotic Pus10 protein sequences to find that Pus10 existed as a single copy gene in all the surveyed genomes despite ancestral whole genome duplications had occurred. This indicates a possible deleterious gene dosage effect. Our results suggest that functional redundancy result in gene loss or neofunctionalization in different evolutionary lineages.</description><subject>Animal Genetics and Genomics</subject><subject>Apoptosis</subject><subject>Archaea</subject><subject>Bacteria</subject><subject>Batrachochytrium</subject><subject>Biomedical and Life Sciences</subject><subject>Catalysis</subject><subject>Cell Biology</subject><subject>Eukaryotes</subject><subject>Evolution</subject><subject>Evolutionary Biology</subject><subject>Fungi</subject><subject>Gene dosage</subject><subject>Gene sequencing</subject><subject>Genes</subject><subject>Genomes</subject><subject>Life Sciences</subject><subject>Microbiology</subject><subject>Original Article</subject><subject>Plant Genetics and Genomics</subject><subject>Plant Sciences</subject><subject>Protozoa</subject><subject>Pseudouridine synthase</subject><subject>Redundancy</subject><subject>TRAIL protein</subject><subject>tRNA</subject><subject>Uridine</subject><issn>0022-2844</issn><issn>1432-1432</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp1kUtLAzEUhYMotj5-gBsZcONmNM_JZKOUUh9QsGD3IZ1J2qnTpCYzhf57U1tLFdzkEs53z72XA8AVgncIQn4fIMREpBDlqcgxT9dHoIsowenmOQbdKOMU55R2wFkIcwgRZ4Kcgg4WhAomRBc8DlaubpvK2cSZZNB-KL9WdaJsmfR8MVM6fkZBt6VrfVVWVifva9vMVNDJqA0IXoATo-qgL3f1HIyfBuP-Szp8e37t94ZpwUjWpLkpIDRUMZZhmAleCmFUqQzCtCiENshoxCiblAYqrjSFlBJFJozlgmNKyDl42Nou28lCl4W2jVe1XPpqEReWTlXyt2KrmZy6lWR5Rjhm0eB2Z-DdZ6tDIxdVKHRdK6tdGyQSucggZ9-zbv6g83i8jddFShDEeU5wpNCWKrwLwWuzXwZBuUlHbtORMR25SUeuY8_14RX7jp84IoC3QIiSnWp_MPpf1y8G9pr8</recordid><startdate>2018</startdate><enddate>2018</enddate><creator>Fitzek, 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Sciences</topic><topic>Protozoa</topic><topic>Pseudouridine synthase</topic><topic>Redundancy</topic><topic>TRAIL protein</topic><topic>tRNA</topic><topic>Uridine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fitzek, Elisabeth</creatorcontrib><creatorcontrib>Joardar, Archi</creatorcontrib><creatorcontrib>Gupta, Ramesh</creatorcontrib><creatorcontrib>Geisler, Matt</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase 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Evol</addtitle><date>2018</date><risdate>2018</risdate><volume>86</volume><issue>1</issue><spage>77</spage><epage>89</epage><pages>77-89</pages><issn>0022-2844</issn><eissn>1432-1432</eissn><abstract>In archaea, pseudouridine (Ψ) synthase Pus10 modifies uridine (U) to Ψ at positions 54 and 55 of tRNA. In contrast, Pus10 is not found in bacteria, where modifications at those two positions are carried out by TrmA (U54 to m
5
U54) and TruB (U55 to Ψ55). Many eukaryotes have an apparent redundancy; their genomes contain orthologs of archaeal Pus10 and bacterial TrmA and TruB. Although eukaryal Pus10 genes share a conserved catalytic domain with archaeal Pus10 genes, their biological roles are not clear for the two reasons. First, experimental evidence suggests that human Pus10 participates in apoptosis induced by the tumor necrosis factor-related apoptosis-inducing ligand. Whether the function of human Pus10 is in place or in addition to of Ψ synthesis in tRNA is unknown. Second, Pus10 is found in earlier evolutionary branches of fungi (such as chytrid
Batrachochytrium
) but is absent in all dikaryon fungi surveyed (Ascomycetes and Basidiomycetes). We did a comprehensive analysis of sequenced genomes and found that orthologs of Pus10, TrmA, and TruB were present in all the animals, plants, and protozoa surveyed. This indicates that the common eukaryotic ancestor possesses all the three genes. Next, we examined 116 archaeal and eukaryotic Pus10 protein sequences to find that Pus10 existed as a single copy gene in all the surveyed genomes despite ancestral whole genome duplications had occurred. This indicates a possible deleterious gene dosage effect. Our results suggest that functional redundancy result in gene loss or neofunctionalization in different evolutionary lineages.</abstract><cop>New York</cop><pub>Springer US</pub><pmid>29349599</pmid><doi>10.1007/s00239-018-9827-y</doi><tpages>13</tpages><orcidid>https://orcid.org/0000-0003-1888-4652</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Animal Genetics and Genomics Apoptosis Archaea Bacteria Batrachochytrium Biomedical and Life Sciences Catalysis Cell Biology Eukaryotes Evolution Evolutionary Biology Fungi Gene dosage Gene sequencing Genes Genomes Life Sciences Microbiology Original Article Plant Genetics and Genomics Plant Sciences Protozoa Pseudouridine synthase Redundancy TRAIL protein tRNA Uridine |
title | Evolution of Eukaryal and Archaeal Pseudouridine Synthase Pus10 |
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