The evolution of Class II Aminoacyl-tRNA synthetases and the first code
•A new evolutionary sequence for the catalytic domain of the Class II synthetases.•Two alternate catalytic domain extensions leads to a split of the Class II synthetases associated with the operational code.•The earliest Class II synthetase may form the link between a Thioester world and a Phosphoes...
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| Veröffentlicht in: | FEBS letters 2015-11, Vol.589 (23), p.3499-3507 |
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| creator | Smith, Temple F. Hartman, Hyman |
| description | •A new evolutionary sequence for the catalytic domain of the Class II synthetases.•Two alternate catalytic domain extensions leads to a split of the Class II synthetases associated with the operational code.•The earliest Class II synthetase may form the link between a Thioester world and a Phosphoester world.
Class II Aminoacyl-tRNA synthetases are a set of very ancient multi domain proteins. The evolution of the catalytic domain of Class II synthetases can be reconstructed from three peptidyl-hairpins. Further evolution from this primordial catalytic core leads to a split of the Class II synthetases into two divisions potentially associated with the operational code. The earliest form of this code likely coded predominantly Glycine (Gly), Proline (Pro), Alanine (Ala) and “Lysine”/Aspartic acid (Lys/Asp). There is a paradox in these synthetases beginning with a hairpin structure before the Genetic Code existed. A resolution is found in the suggestion that the primordial Aminoacyl synthetases formed in a transition from a Thioester world to a Phosphate ester world. |
| doi_str_mv | 10.1016/j.febslet.2015.10.006 |
| format | Article |
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Class II Aminoacyl-tRNA synthetases are a set of very ancient multi domain proteins. The evolution of the catalytic domain of Class II synthetases can be reconstructed from three peptidyl-hairpins. Further evolution from this primordial catalytic core leads to a split of the Class II synthetases into two divisions potentially associated with the operational code. The earliest form of this code likely coded predominantly Glycine (Gly), Proline (Pro), Alanine (Ala) and “Lysine”/Aspartic acid (Lys/Asp). There is a paradox in these synthetases beginning with a hairpin structure before the Genetic Code existed. A resolution is found in the suggestion that the primordial Aminoacyl synthetases formed in a transition from a Thioester world to a Phosphate ester world.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2015.10.006</identifier><identifier>PMID: 26472323</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Amino Acyl-tRNA Synthetases - chemistry ; Amino Acyl-tRNA Synthetases - metabolism ; Aminoacyl-tRNA-synthetase ; Catalytic Domain ; Evolution ; Evolution, Molecular ; Models, Molecular ; Operational-code ; Thioester</subject><ispartof>FEBS letters, 2015-11, Vol.589 (23), p.3499-3507</ispartof><rights>2015 Federation of European Biochemical Societies</rights><rights>FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5438-d285d5c084f7f843624a94c0d161530856d81b485fde29089c1b929469f6a66b3</citedby><cites>FETCH-LOGICAL-c5438-d285d5c084f7f843624a94c0d161530856d81b485fde29089c1b929469f6a66b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2015.10.006$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579315008868$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3537,27901,27902,45550,45551,46384,46808,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26472323$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Smith, Temple F.</creatorcontrib><creatorcontrib>Hartman, Hyman</creatorcontrib><title>The evolution of Class II Aminoacyl-tRNA synthetases and the first code</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>•A new evolutionary sequence for the catalytic domain of the Class II synthetases.•Two alternate catalytic domain extensions leads to a split of the Class II synthetases associated with the operational code.•The earliest Class II synthetase may form the link between a Thioester world and a Phosphoester world.
Class II Aminoacyl-tRNA synthetases are a set of very ancient multi domain proteins. The evolution of the catalytic domain of Class II synthetases can be reconstructed from three peptidyl-hairpins. Further evolution from this primordial catalytic core leads to a split of the Class II synthetases into two divisions potentially associated with the operational code. The earliest form of this code likely coded predominantly Glycine (Gly), Proline (Pro), Alanine (Ala) and “Lysine”/Aspartic acid (Lys/Asp). There is a paradox in these synthetases beginning with a hairpin structure before the Genetic Code existed. A resolution is found in the suggestion that the primordial Aminoacyl synthetases formed in a transition from a Thioester world to a Phosphate ester world.</description><subject>Amino Acyl-tRNA Synthetases - chemistry</subject><subject>Amino Acyl-tRNA Synthetases - metabolism</subject><subject>Aminoacyl-tRNA-synthetase</subject><subject>Catalytic Domain</subject><subject>Evolution</subject><subject>Evolution, Molecular</subject><subject>Models, Molecular</subject><subject>Operational-code</subject><subject>Thioester</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU1rGzEQhkVpaRy3PyFBx17W1fdqT8Ex-TCEFtr0LLTSiMisV8lqneB_Hy12ck1PYoZ3Hg3PIHRGyYISqn5uFgHa3MG4YITK0lsQoj6hGdU1r7hQ-jOaEUJFJeuGn6DTnDek1Jo2X9EJU6JmnPEZurl_AAzPqduNMfU4BbzqbM54vcbLbeyTdfuuGv_8WuK878cHGG2GjG3vcSlwiEMesUsevqEvwXYZvh_fOfp3fXW_uq3uft-sV8u7yknBdeWZll46okWogxZcMWEb4YinikpOtFRe01ZoGTywhujG0bZhjVBNUFapls_RjwP3cUhPO8ij2cbsoOtsD2mXDa255Jzywp4jeYi6IeU8QDCPQ9zaYW8oMZNDszFHh2ZyOLWLwzJ3fvxi127Bv0-9SSuB20PgJXaw_z-qub66ZH-ng0z3oJIQrZUuqIsDCoqz5wiDyS5C78DHAdxofIofbPsKAEKYMg</recordid><startdate>20151130</startdate><enddate>20151130</enddate><creator>Smith, Temple F.</creator><creator>Hartman, Hyman</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><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>7X8</scope></search><sort><creationdate>20151130</creationdate><title>The evolution of Class II Aminoacyl-tRNA synthetases and the first code</title><author>Smith, Temple F. ; Hartman, Hyman</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5438-d285d5c084f7f843624a94c0d161530856d81b485fde29089c1b929469f6a66b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Amino Acyl-tRNA Synthetases - chemistry</topic><topic>Amino Acyl-tRNA Synthetases - metabolism</topic><topic>Aminoacyl-tRNA-synthetase</topic><topic>Catalytic Domain</topic><topic>Evolution</topic><topic>Evolution, Molecular</topic><topic>Models, Molecular</topic><topic>Operational-code</topic><topic>Thioester</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Smith, Temple F.</creatorcontrib><creatorcontrib>Hartman, Hyman</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Smith, Temple F.</au><au>Hartman, Hyman</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The evolution of Class II Aminoacyl-tRNA synthetases and the first code</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2015-11-30</date><risdate>2015</risdate><volume>589</volume><issue>23</issue><spage>3499</spage><epage>3507</epage><pages>3499-3507</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>•A new evolutionary sequence for the catalytic domain of the Class II synthetases.•Two alternate catalytic domain extensions leads to a split of the Class II synthetases associated with the operational code.•The earliest Class II synthetase may form the link between a Thioester world and a Phosphoester world.
Class II Aminoacyl-tRNA synthetases are a set of very ancient multi domain proteins. The evolution of the catalytic domain of Class II synthetases can be reconstructed from three peptidyl-hairpins. Further evolution from this primordial catalytic core leads to a split of the Class II synthetases into two divisions potentially associated with the operational code. The earliest form of this code likely coded predominantly Glycine (Gly), Proline (Pro), Alanine (Ala) and “Lysine”/Aspartic acid (Lys/Asp). There is a paradox in these synthetases beginning with a hairpin structure before the Genetic Code existed. A resolution is found in the suggestion that the primordial Aminoacyl synthetases formed in a transition from a Thioester world to a Phosphate ester world.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>26472323</pmid><doi>10.1016/j.febslet.2015.10.006</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acyl-tRNA Synthetases - chemistry Amino Acyl-tRNA Synthetases - metabolism Aminoacyl-tRNA-synthetase Catalytic Domain Evolution Evolution, Molecular Models, Molecular Operational-code Thioester |
| title | The evolution of Class II Aminoacyl-tRNA synthetases and the first code |
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