Evolution of genes, evolution of species: the case of aminoacyl-tRNA synthetases
All of the aminoacyl-tRNA synthetase (aaRS) sequences currently available in the data banks have been subjected to a systematic analysis aimed at finding gene duplications, genetic recombinations, and horizontal transfers. Evidence is provided for the occurrence (or probable occurrence) of such phen...
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Veröffentlicht in: | Molecular biology and evolution 1998-11, Vol.15 (11), p.1548-1561 |
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creator | Diaz-Lazcoz, Y Aude, J C Nitschké, P Chiapello, H Landès-Devauchelle, C Risler, J L |
description | All of the aminoacyl-tRNA synthetase (aaRS) sequences currently available in the data banks have been subjected to a systematic analysis aimed at finding gene duplications, genetic recombinations, and horizontal transfers. Evidence is provided for the occurrence (or probable occurrence) of such phenomena within this class of enzymes. In particular, it is suggested that the monomeric PheRS from the yeast mitochondrion is a chimera of the alpha and beta chains of the standard tetrameric protein. In addition, it is proposed that the dimeric and tetrameric forms of GlyRS are the result of a double and independent acquisition of the same specificity within two different subclasses of aaRS. The phylogenetic reconstructions of the evolutionary histories of the genes encoding aaRS are shown to be extremely diverse. While large segments of the population are consistent with the broad grouping into the three Woesian domains, some phylogenetic reconstructions do not place the Archae and the Eucarya as sister groups but, rather, show a gram-negative bacteria/eukaryote clustering. In addition, many individual genes pose difficulties that preclude any simple evolutionary scheme. Thus, aaRS's are clearly a paradigm of F. Jacob's "odd jobs of evolution" but, on the whole, do not call into question the evolutionary scenario originally proposed by Woese and subsequently refined by others. |
doi_str_mv | 10.1093/oxfordjournals.molbev.a025882 |
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Evidence is provided for the occurrence (or probable occurrence) of such phenomena within this class of enzymes. In particular, it is suggested that the monomeric PheRS from the yeast mitochondrion is a chimera of the alpha and beta chains of the standard tetrameric protein. In addition, it is proposed that the dimeric and tetrameric forms of GlyRS are the result of a double and independent acquisition of the same specificity within two different subclasses of aaRS. The phylogenetic reconstructions of the evolutionary histories of the genes encoding aaRS are shown to be extremely diverse. While large segments of the population are consistent with the broad grouping into the three Woesian domains, some phylogenetic reconstructions do not place the Archae and the Eucarya as sister groups but, rather, show a gram-negative bacteria/eukaryote clustering. In addition, many individual genes pose difficulties that preclude any simple evolutionary scheme. 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Jacob's "odd jobs of evolution" but, on the whole, do not call into question the evolutionary scenario originally proposed by Woese and subsequently refined by others.</description><identifier>ISSN: 0737-4038</identifier><identifier>EISSN: 1537-1719</identifier><identifier>DOI: 10.1093/oxfordjournals.molbev.a025882</identifier><identifier>PMID: 12572618</identifier><language>eng</language><publisher>United States</publisher><subject>Amino Acid Sequence ; Amino Acyl-tRNA Synthetases - classification ; Amino Acyl-tRNA Synthetases - genetics ; Animals ; Archaea ; Cattle ; Cricetinae ; Evolution, Molecular ; Genes - genetics ; Genes, Archaeal - genetics ; Genes, Bacterial - genetics ; Genes, Fungal - genetics ; Genes, Helminth - genetics ; Glycine-tRNA Ligase - classification ; Glycine-tRNA Ligase - genetics ; Humans ; Mice ; Mitochondrial Proteins - genetics ; Molecular Sequence Data ; Rabbits ; RNA, Transfer, Amino Acid-Specific - classification ; RNA, Transfer, Amino Acid-Specific - genetics ; Sequence Alignment - methods ; Species Specificity ; Tryptophan-tRNA Ligase - classification ; Tryptophan-tRNA Ligase - genetics ; Tyrosine-tRNA Ligase - classification ; Tyrosine-tRNA Ligase - genetics</subject><ispartof>Molecular biology and evolution, 1998-11, Vol.15 (11), p.1548-1561</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c456t-f87b3e6b55528f148e73042f4c90f8f83a125480bce539dee18304bda0b09d053</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,1598,27901,27902</link.rule.ids><linktorsrc>$$Uhttps://dx.doi.org/10.1093/oxfordjournals.molbev.a025882$$EView_record_in_Oxford_University_Press$$FView_record_in_$$GOxford_University_Press</linktorsrc><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12572618$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Diaz-Lazcoz, Y</creatorcontrib><creatorcontrib>Aude, J C</creatorcontrib><creatorcontrib>Nitschké, P</creatorcontrib><creatorcontrib>Chiapello, H</creatorcontrib><creatorcontrib>Landès-Devauchelle, C</creatorcontrib><creatorcontrib>Risler, J L</creatorcontrib><title>Evolution of genes, evolution of species: the case of aminoacyl-tRNA synthetases</title><title>Molecular biology and evolution</title><addtitle>Mol Biol Evol</addtitle><description>All of the aminoacyl-tRNA synthetase (aaRS) sequences currently available in the data banks have been subjected to a systematic analysis aimed at finding gene duplications, genetic recombinations, and horizontal transfers. Evidence is provided for the occurrence (or probable occurrence) of such phenomena within this class of enzymes. In particular, it is suggested that the monomeric PheRS from the yeast mitochondrion is a chimera of the alpha and beta chains of the standard tetrameric protein. In addition, it is proposed that the dimeric and tetrameric forms of GlyRS are the result of a double and independent acquisition of the same specificity within two different subclasses of aaRS. The phylogenetic reconstructions of the evolutionary histories of the genes encoding aaRS are shown to be extremely diverse. While large segments of the population are consistent with the broad grouping into the three Woesian domains, some phylogenetic reconstructions do not place the Archae and the Eucarya as sister groups but, rather, show a gram-negative bacteria/eukaryote clustering. In addition, many individual genes pose difficulties that preclude any simple evolutionary scheme. 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Jacob's "odd jobs of evolution" but, on the whole, do not call into question the evolutionary scenario originally proposed by Woese and subsequently refined by others.</description><subject>Amino Acid Sequence</subject><subject>Amino Acyl-tRNA Synthetases - classification</subject><subject>Amino Acyl-tRNA Synthetases - genetics</subject><subject>Animals</subject><subject>Archaea</subject><subject>Cattle</subject><subject>Cricetinae</subject><subject>Evolution, Molecular</subject><subject>Genes - genetics</subject><subject>Genes, Archaeal - genetics</subject><subject>Genes, Bacterial - genetics</subject><subject>Genes, Fungal - genetics</subject><subject>Genes, Helminth - genetics</subject><subject>Glycine-tRNA Ligase - classification</subject><subject>Glycine-tRNA Ligase - genetics</subject><subject>Humans</subject><subject>Mice</subject><subject>Mitochondrial Proteins - genetics</subject><subject>Molecular Sequence Data</subject><subject>Rabbits</subject><subject>RNA, Transfer, Amino Acid-Specific - classification</subject><subject>RNA, Transfer, Amino Acid-Specific - genetics</subject><subject>Sequence Alignment - methods</subject><subject>Species Specificity</subject><subject>Tryptophan-tRNA Ligase - classification</subject><subject>Tryptophan-tRNA Ligase - genetics</subject><subject>Tyrosine-tRNA Ligase - classification</subject><subject>Tyrosine-tRNA Ligase - genetics</subject><issn>0737-4038</issn><issn>1537-1719</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkF1LwzAUhoMobk7_gvRGr-xMmqRJBS_GmB8wVESvQ9qeaEfbzKYd7t-b0YJ6JV4lnPc5HzwInRE8JTihl_bT2CZf2a6pdemmlS1T2Ew1jriU0R4aE05FSARJ9tEYC_9nmMoROnJuhTFhLI4P0YhEXEQxkWP0tNjYsmsLWwfWBG9Qg7sI4GfNrSErwF0F7TsEmXawK-qqqK3OtmXYPj_MAretfdr60B2jA-MPg5PhnaDXm8XL_C5cPt7ez2fLMGM8bkMjRUohTjnnkTSESRAUs8iwLMFGGkm1v5FJnGbAaZIDEOnzNNc4xUmOOZ2g837uurEfHbhWVYXLoCx1DbZzSiQxpVLQP0HvSmCSYA9e92DWWOcaMGrdFJVutopgtXOvfrtXvXs1uPf9p8OiLq0g_-4eZHtA9oDt1v-c_QXjG5wR</recordid><startdate>19981101</startdate><enddate>19981101</enddate><creator>Diaz-Lazcoz, Y</creator><creator>Aude, J C</creator><creator>Nitschké, P</creator><creator>Chiapello, H</creator><creator>Landès-Devauchelle, C</creator><creator>Risler, J L</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19981101</creationdate><title>Evolution of genes, evolution of species: the case of aminoacyl-tRNA synthetases</title><author>Diaz-Lazcoz, Y ; Aude, J C ; Nitschké, P ; Chiapello, H ; Landès-Devauchelle, C ; Risler, J L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c456t-f87b3e6b55528f148e73042f4c90f8f83a125480bce539dee18304bda0b09d053</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Amino Acid Sequence</topic><topic>Amino Acyl-tRNA Synthetases - classification</topic><topic>Amino Acyl-tRNA Synthetases - genetics</topic><topic>Animals</topic><topic>Archaea</topic><topic>Cattle</topic><topic>Cricetinae</topic><topic>Evolution, Molecular</topic><topic>Genes - genetics</topic><topic>Genes, Archaeal - genetics</topic><topic>Genes, Bacterial - genetics</topic><topic>Genes, Fungal - genetics</topic><topic>Genes, Helminth - genetics</topic><topic>Glycine-tRNA Ligase - classification</topic><topic>Glycine-tRNA Ligase - genetics</topic><topic>Humans</topic><topic>Mice</topic><topic>Mitochondrial Proteins - genetics</topic><topic>Molecular Sequence Data</topic><topic>Rabbits</topic><topic>RNA, Transfer, Amino Acid-Specific - classification</topic><topic>RNA, Transfer, Amino Acid-Specific - genetics</topic><topic>Sequence Alignment - methods</topic><topic>Species Specificity</topic><topic>Tryptophan-tRNA Ligase - classification</topic><topic>Tryptophan-tRNA Ligase - genetics</topic><topic>Tyrosine-tRNA Ligase - classification</topic><topic>Tyrosine-tRNA Ligase - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Diaz-Lazcoz, Y</creatorcontrib><creatorcontrib>Aude, J C</creatorcontrib><creatorcontrib>Nitschké, P</creatorcontrib><creatorcontrib>Chiapello, H</creatorcontrib><creatorcontrib>Landès-Devauchelle, C</creatorcontrib><creatorcontrib>Risler, J L</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular biology and evolution</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Diaz-Lazcoz, Y</au><au>Aude, J C</au><au>Nitschké, P</au><au>Chiapello, H</au><au>Landès-Devauchelle, C</au><au>Risler, J L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Evolution of genes, evolution of species: the case of aminoacyl-tRNA synthetases</atitle><jtitle>Molecular biology and evolution</jtitle><addtitle>Mol Biol Evol</addtitle><date>1998-11-01</date><risdate>1998</risdate><volume>15</volume><issue>11</issue><spage>1548</spage><epage>1561</epage><pages>1548-1561</pages><issn>0737-4038</issn><eissn>1537-1719</eissn><abstract>All of the aminoacyl-tRNA synthetase (aaRS) sequences currently available in the data banks have been subjected to a systematic analysis aimed at finding gene duplications, genetic recombinations, and horizontal transfers. Evidence is provided for the occurrence (or probable occurrence) of such phenomena within this class of enzymes. In particular, it is suggested that the monomeric PheRS from the yeast mitochondrion is a chimera of the alpha and beta chains of the standard tetrameric protein. In addition, it is proposed that the dimeric and tetrameric forms of GlyRS are the result of a double and independent acquisition of the same specificity within two different subclasses of aaRS. The phylogenetic reconstructions of the evolutionary histories of the genes encoding aaRS are shown to be extremely diverse. While large segments of the population are consistent with the broad grouping into the three Woesian domains, some phylogenetic reconstructions do not place the Archae and the Eucarya as sister groups but, rather, show a gram-negative bacteria/eukaryote clustering. In addition, many individual genes pose difficulties that preclude any simple evolutionary scheme. Thus, aaRS's are clearly a paradigm of F. Jacob's "odd jobs of evolution" but, on the whole, do not call into question the evolutionary scenario originally proposed by Woese and subsequently refined by others.</abstract><cop>United States</cop><pmid>12572618</pmid><doi>10.1093/oxfordjournals.molbev.a025882</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Amino Acyl-tRNA Synthetases - classification Amino Acyl-tRNA Synthetases - genetics Animals Archaea Cattle Cricetinae Evolution, Molecular Genes - genetics Genes, Archaeal - genetics Genes, Bacterial - genetics Genes, Fungal - genetics Genes, Helminth - genetics Glycine-tRNA Ligase - classification Glycine-tRNA Ligase - genetics Humans Mice Mitochondrial Proteins - genetics Molecular Sequence Data Rabbits RNA, Transfer, Amino Acid-Specific - classification RNA, Transfer, Amino Acid-Specific - genetics Sequence Alignment - methods Species Specificity Tryptophan-tRNA Ligase - classification Tryptophan-tRNA Ligase - genetics Tyrosine-tRNA Ligase - classification Tyrosine-tRNA Ligase - genetics |
title | Evolution of genes, evolution of species: the case of aminoacyl-tRNA synthetases |
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