Aminoacyl-tRNA Synthetases and tRNAs for an Expanded Genetic Code: What Makes them Orthogonal?

In the past two decades, tRNA molecules and their corresponding aminoacyl-tRNA synthetases (aaRS) have been extensively used in synthetic biology to genetically encode post-translationally modified and unnatural amino acids. In this review, we briefly examine one fundamental requirement for the succ...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:International journal of molecular sciences 2019-04, Vol.20 (8), p.1929
Hauptverfasser: Melnikov, Sergey V, Söll, Dieter
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page
container_issue 8
container_start_page 1929
container_title International journal of molecular sciences
container_volume 20
creator Melnikov, Sergey V
Söll, Dieter
description In the past two decades, tRNA molecules and their corresponding aminoacyl-tRNA synthetases (aaRS) have been extensively used in synthetic biology to genetically encode post-translationally modified and unnatural amino acids. In this review, we briefly examine one fundamental requirement for the successful application of tRNA/aaRS pairs for expanding the genetic code. This requirement is known as "orthogonality"-the ability of a tRNA and its corresponding aaRS to interact exclusively with each other and avoid cross-reactions with additional types of tRNAs and aaRSs in a given organism.
doi_str_mv 10.3390/ijms20081929
format Article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6515474</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2332335253</sourcerecordid><originalsourceid>FETCH-LOGICAL-c478t-bff0c2316a304ab5dd69df18c32238d57ddbd5d81c26eeda94a0234ceafc91743</originalsourceid><addsrcrecordid>eNpdkUtLAzEUhYMotlZ3riXgxoWjeUymMy6UUmoV1IIP3BnSJNNOnZnUJBX7701tLVUSyM3Ndw85HAAOMTqjNEPnxaRyBKEUZyTbAk0cExIhlLS3N-oG2HNughChhGW7oEExCovQJnjrVEVthJyXkX986MCnee3H2gunHRS1goumg7mx4QZ7X9PQ0wr2da19IWHXKH0BX8fCw3vxHkbCbAUH1o_NyNSivNoHO7konT5YnS3wct177t5Ed4P-bbdzF8m4nfpomOdIEooTQVEshkypJFM5TiUlhKaKtZUaKqZSLEmitRJZLIKXWGqRywy3Y9oCl0vd6WxYaSV17a0o-dQWlbBzbkTB_77UxZiPzCdPGGbxj8DJSsCaj5l2nleFk7osRa3NzHFCMA0kYQv0-B86MTMb3AaK0rAZYTRQp0tKWuOc1fn6MxjxRXB8M7iAH20aWMO_SdFvAgeUNA</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2332335253</pqid></control><display><type>article</type><title>Aminoacyl-tRNA Synthetases and tRNAs for an Expanded Genetic Code: What Makes them Orthogonal?</title><source>MDPI - Multidisciplinary Digital Publishing Institute</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>PubMed Central</source><creator>Melnikov, Sergey V ; Söll, Dieter</creator><creatorcontrib>Melnikov, Sergey V ; Söll, Dieter</creatorcontrib><description>In the past two decades, tRNA molecules and their corresponding aminoacyl-tRNA synthetases (aaRS) have been extensively used in synthetic biology to genetically encode post-translationally modified and unnatural amino acids. In this review, we briefly examine one fundamental requirement for the successful application of tRNA/aaRS pairs for expanding the genetic code. This requirement is known as "orthogonality"-the ability of a tRNA and its corresponding aaRS to interact exclusively with each other and avoid cross-reactions with additional types of tRNAs and aaRSs in a given organism.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms20081929</identifier><identifier>PMID: 31010123</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Alanine ; Alanine-tRNA ligase ; Amino acids ; Aminoacylation ; Bacteria ; Catalytic activity ; Codons ; E coli ; Evolution ; Genetic code ; Genetic engineering ; Genomes ; Leucine ; Morphogenesis ; Orthogonality ; Phages ; Proteins ; Review ; Serine ; Substrate specificity ; Transplantation ; tRNA ; Virulence</subject><ispartof>International journal of molecular sciences, 2019-04, Vol.20 (8), p.1929</ispartof><rights>2019. This work is licensed under https://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2019 by the authors. 2019</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c478t-bff0c2316a304ab5dd69df18c32238d57ddbd5d81c26eeda94a0234ceafc91743</citedby><cites>FETCH-LOGICAL-c478t-bff0c2316a304ab5dd69df18c32238d57ddbd5d81c26eeda94a0234ceafc91743</cites><orcidid>0000-0002-3077-8986</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6515474/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6515474/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27903,27904,53769,53771</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31010123$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Melnikov, Sergey V</creatorcontrib><creatorcontrib>Söll, Dieter</creatorcontrib><title>Aminoacyl-tRNA Synthetases and tRNAs for an Expanded Genetic Code: What Makes them Orthogonal?</title><title>International journal of molecular sciences</title><addtitle>Int J Mol Sci</addtitle><description>In the past two decades, tRNA molecules and their corresponding aminoacyl-tRNA synthetases (aaRS) have been extensively used in synthetic biology to genetically encode post-translationally modified and unnatural amino acids. In this review, we briefly examine one fundamental requirement for the successful application of tRNA/aaRS pairs for expanding the genetic code. This requirement is known as "orthogonality"-the ability of a tRNA and its corresponding aaRS to interact exclusively with each other and avoid cross-reactions with additional types of tRNAs and aaRSs in a given organism.</description><subject>Alanine</subject><subject>Alanine-tRNA ligase</subject><subject>Amino acids</subject><subject>Aminoacylation</subject><subject>Bacteria</subject><subject>Catalytic activity</subject><subject>Codons</subject><subject>E coli</subject><subject>Evolution</subject><subject>Genetic code</subject><subject>Genetic engineering</subject><subject>Genomes</subject><subject>Leucine</subject><subject>Morphogenesis</subject><subject>Orthogonality</subject><subject>Phages</subject><subject>Proteins</subject><subject>Review</subject><subject>Serine</subject><subject>Substrate specificity</subject><subject>Transplantation</subject><subject>tRNA</subject><subject>Virulence</subject><issn>1422-0067</issn><issn>1661-6596</issn><issn>1422-0067</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpdkUtLAzEUhYMotlZ3riXgxoWjeUymMy6UUmoV1IIP3BnSJNNOnZnUJBX7701tLVUSyM3Ndw85HAAOMTqjNEPnxaRyBKEUZyTbAk0cExIhlLS3N-oG2HNughChhGW7oEExCovQJnjrVEVthJyXkX986MCnee3H2gunHRS1goumg7mx4QZ7X9PQ0wr2da19IWHXKH0BX8fCw3vxHkbCbAUH1o_NyNSivNoHO7konT5YnS3wct177t5Ed4P-bbdzF8m4nfpomOdIEooTQVEshkypJFM5TiUlhKaKtZUaKqZSLEmitRJZLIKXWGqRywy3Y9oCl0vd6WxYaSV17a0o-dQWlbBzbkTB_77UxZiPzCdPGGbxj8DJSsCaj5l2nleFk7osRa3NzHFCMA0kYQv0-B86MTMb3AaK0rAZYTRQp0tKWuOc1fn6MxjxRXB8M7iAH20aWMO_SdFvAgeUNA</recordid><startdate>20190419</startdate><enddate>20190419</enddate><creator>Melnikov, Sergey V</creator><creator>Söll, Dieter</creator><general>MDPI AG</general><general>MDPI</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-3077-8986</orcidid></search><sort><creationdate>20190419</creationdate><title>Aminoacyl-tRNA Synthetases and tRNAs for an Expanded Genetic Code: What Makes them Orthogonal?</title><author>Melnikov, Sergey V ; Söll, Dieter</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c478t-bff0c2316a304ab5dd69df18c32238d57ddbd5d81c26eeda94a0234ceafc91743</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Alanine</topic><topic>Alanine-tRNA ligase</topic><topic>Amino acids</topic><topic>Aminoacylation</topic><topic>Bacteria</topic><topic>Catalytic activity</topic><topic>Codons</topic><topic>E coli</topic><topic>Evolution</topic><topic>Genetic code</topic><topic>Genetic engineering</topic><topic>Genomes</topic><topic>Leucine</topic><topic>Morphogenesis</topic><topic>Orthogonality</topic><topic>Phages</topic><topic>Proteins</topic><topic>Review</topic><topic>Serine</topic><topic>Substrate specificity</topic><topic>Transplantation</topic><topic>tRNA</topic><topic>Virulence</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Melnikov, Sergey V</creatorcontrib><creatorcontrib>Söll, Dieter</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health &amp; Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Research Library (Corporate)</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>International journal of molecular sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Melnikov, Sergey V</au><au>Söll, Dieter</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Aminoacyl-tRNA Synthetases and tRNAs for an Expanded Genetic Code: What Makes them Orthogonal?</atitle><jtitle>International journal of molecular sciences</jtitle><addtitle>Int J Mol Sci</addtitle><date>2019-04-19</date><risdate>2019</risdate><volume>20</volume><issue>8</issue><spage>1929</spage><pages>1929-</pages><issn>1422-0067</issn><issn>1661-6596</issn><eissn>1422-0067</eissn><abstract>In the past two decades, tRNA molecules and their corresponding aminoacyl-tRNA synthetases (aaRS) have been extensively used in synthetic biology to genetically encode post-translationally modified and unnatural amino acids. In this review, we briefly examine one fundamental requirement for the successful application of tRNA/aaRS pairs for expanding the genetic code. This requirement is known as "orthogonality"-the ability of a tRNA and its corresponding aaRS to interact exclusively with each other and avoid cross-reactions with additional types of tRNAs and aaRSs in a given organism.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>31010123</pmid><doi>10.3390/ijms20081929</doi><orcidid>https://orcid.org/0000-0002-3077-8986</orcidid><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 1422-0067
ispartof International journal of molecular sciences, 2019-04, Vol.20 (8), p.1929
issn 1422-0067
1661-6596
1422-0067
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6515474
source MDPI - Multidisciplinary Digital Publishing Institute; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central
subjects Alanine
Alanine-tRNA ligase
Amino acids
Aminoacylation
Bacteria
Catalytic activity
Codons
E coli
Evolution
Genetic code
Genetic engineering
Genomes
Leucine
Morphogenesis
Orthogonality
Phages
Proteins
Review
Serine
Substrate specificity
Transplantation
tRNA
Virulence
title Aminoacyl-tRNA Synthetases and tRNAs for an Expanded Genetic Code: What Makes them Orthogonal?
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-27T03%3A44%3A36IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Aminoacyl-tRNA%20Synthetases%20and%20tRNAs%20for%20an%20Expanded%20Genetic%20Code:%20What%20Makes%20them%20Orthogonal?&rft.jtitle=International%20journal%20of%20molecular%20sciences&rft.au=Melnikov,%20Sergey%20V&rft.date=2019-04-19&rft.volume=20&rft.issue=8&rft.spage=1929&rft.pages=1929-&rft.issn=1422-0067&rft.eissn=1422-0067&rft_id=info:doi/10.3390/ijms20081929&rft_dat=%3Cproquest_pubme%3E2332335253%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2332335253&rft_id=info:pmid/31010123&rfr_iscdi=true