Crystal structure of Nanoarchaeum equitans tyrosyl-tRNA synthetase and its aminoacylation activity toward tRNA Tyr with an extra guanosine residue at the 5'-terminus
tRNA of Nanoarchaeum equitans has a remarkable feature with an extra guanosine residue at the 5'-terminus. However, the N. equitans tRNA mutant without extra guanosine at the 5'-end was tyrosylated by tyrosyl-tRNA synthase (TyrRS). We solved the crystal structure of N. equitans TyrRS at 2....
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| Veröffentlicht in: | Biochemical and biophysical research communications 2021-10, Vol.575, p.90 |
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| creator | Horikoshi, Tatsuya Noguchi, Hiroki Umehara, Takuya Mutsuro-Aoki, Hiromi Kurihara, Ryodai Noguchi, Ryohei Hashimoto, Takahiro Watanabe, Yuki Ando, Tadashi Kamata, Kenichi Park, Sam-Yong Tamura, Koji |
| description | tRNA
of Nanoarchaeum equitans has a remarkable feature with an extra guanosine residue at the 5'-terminus. However, the N. equitans tRNA
mutant without extra guanosine at the 5'-end was tyrosylated by tyrosyl-tRNA synthase (TyrRS). We solved the crystal structure of N. equitans TyrRS at 2.80 Å resolution. By comparing the present solved structure with the complex structures TyrRS with tRNA
of Thermus thermophilus and Methanocaldococcus jannaschii, an arginine substitution mutant of N. equitans TyrRS at Ile200 (I200R), which is the putative closest candidate to the 5'-phosphate of C1 of N. equitans tRNA
, was prepared. The I200R mutant tyrosylated not only wild-type tRNA
but also the tRNA without the G-1 residue. Further tyrosylation analysis revealed that the second base of the anticodon (U35), discriminator base (A73), and C1:G72 base pair are strong recognition sites. |
| format | Article |
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of Nanoarchaeum equitans has a remarkable feature with an extra guanosine residue at the 5'-terminus. However, the N. equitans tRNA
mutant without extra guanosine at the 5'-end was tyrosylated by tyrosyl-tRNA synthase (TyrRS). We solved the crystal structure of N. equitans TyrRS at 2.80 Å resolution. By comparing the present solved structure with the complex structures TyrRS with tRNA
of Thermus thermophilus and Methanocaldococcus jannaschii, an arginine substitution mutant of N. equitans TyrRS at Ile200 (I200R), which is the putative closest candidate to the 5'-phosphate of C1 of N. equitans tRNA
, was prepared. The I200R mutant tyrosylated not only wild-type tRNA
but also the tRNA without the G-1 residue. Further tyrosylation analysis revealed that the second base of the anticodon (U35), discriminator base (A73), and C1:G72 base pair are strong recognition sites.</description><identifier>EISSN: 1090-2104</identifier><identifier>PMID: 34461441</identifier><language>eng</language><publisher>United States</publisher><subject>Aminoacylation ; Archaeal Proteins - chemistry ; Archaeal Proteins - genetics ; Archaeal Proteins - metabolism ; Crystallography, X-Ray - methods ; Guanosine - chemistry ; Models, Molecular ; Nanoarchaeota - enzymology ; Protein Structural Elements ; RNA, Transfer, Tyr - chemistry ; RNA, Transfer, Tyr - genetics ; RNA, Transfer, Tyr - metabolism ; Tyrosine-tRNA Ligase - chemistry ; Tyrosine-tRNA Ligase - genetics ; Tyrosine-tRNA Ligase - metabolism</subject><ispartof>Biochemical and biophysical research communications, 2021-10, Vol.575, p.90</ispartof><rights>Copyright © 2021 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34461441$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Horikoshi, Tatsuya</creatorcontrib><creatorcontrib>Noguchi, Hiroki</creatorcontrib><creatorcontrib>Umehara, Takuya</creatorcontrib><creatorcontrib>Mutsuro-Aoki, Hiromi</creatorcontrib><creatorcontrib>Kurihara, Ryodai</creatorcontrib><creatorcontrib>Noguchi, Ryohei</creatorcontrib><creatorcontrib>Hashimoto, Takahiro</creatorcontrib><creatorcontrib>Watanabe, Yuki</creatorcontrib><creatorcontrib>Ando, Tadashi</creatorcontrib><creatorcontrib>Kamata, Kenichi</creatorcontrib><creatorcontrib>Park, Sam-Yong</creatorcontrib><creatorcontrib>Tamura, Koji</creatorcontrib><title>Crystal structure of Nanoarchaeum equitans tyrosyl-tRNA synthetase and its aminoacylation activity toward tRNA Tyr with an extra guanosine residue at the 5'-terminus</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>tRNA
of Nanoarchaeum equitans has a remarkable feature with an extra guanosine residue at the 5'-terminus. However, the N. equitans tRNA
mutant without extra guanosine at the 5'-end was tyrosylated by tyrosyl-tRNA synthase (TyrRS). We solved the crystal structure of N. equitans TyrRS at 2.80 Å resolution. By comparing the present solved structure with the complex structures TyrRS with tRNA
of Thermus thermophilus and Methanocaldococcus jannaschii, an arginine substitution mutant of N. equitans TyrRS at Ile200 (I200R), which is the putative closest candidate to the 5'-phosphate of C1 of N. equitans tRNA
, was prepared. The I200R mutant tyrosylated not only wild-type tRNA
but also the tRNA without the G-1 residue. Further tyrosylation analysis revealed that the second base of the anticodon (U35), discriminator base (A73), and C1:G72 base pair are strong recognition sites.</description><subject>Aminoacylation</subject><subject>Archaeal Proteins - chemistry</subject><subject>Archaeal Proteins - genetics</subject><subject>Archaeal Proteins - metabolism</subject><subject>Crystallography, X-Ray - methods</subject><subject>Guanosine - chemistry</subject><subject>Models, Molecular</subject><subject>Nanoarchaeota - enzymology</subject><subject>Protein Structural Elements</subject><subject>RNA, Transfer, Tyr - chemistry</subject><subject>RNA, Transfer, Tyr - genetics</subject><subject>RNA, Transfer, Tyr - metabolism</subject><subject>Tyrosine-tRNA Ligase - chemistry</subject><subject>Tyrosine-tRNA Ligase - genetics</subject><subject>Tyrosine-tRNA Ligase - metabolism</subject><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFj81KA0EQhAdBTPx5Bembp4UdMwZylKB4ykFyD-1ux23ZnYndPcZ5IN_TQfTsqS71fUWduLlvV21z69swc-eqb23rfViuztxsEcLSh-Dn7mstRQ1HUJPcWRaCtIcNxoTSDUh5AnrPbBgVrEjSMjb2vLkHLdEGMlQCjD2wKeDEFevKiMYpAnbGH2wFLB1RevjBtkXgyDZUCOjTBOE11zHlSCCk3OfqM6hquLtpjKQ6s1660z2OSle_eeGuHx-266fmkF8m6ncH4Qml7P5-Lf4tfAMcnFyc</recordid><startdate>20211020</startdate><enddate>20211020</enddate><creator>Horikoshi, Tatsuya</creator><creator>Noguchi, Hiroki</creator><creator>Umehara, Takuya</creator><creator>Mutsuro-Aoki, Hiromi</creator><creator>Kurihara, Ryodai</creator><creator>Noguchi, Ryohei</creator><creator>Hashimoto, Takahiro</creator><creator>Watanabe, Yuki</creator><creator>Ando, Tadashi</creator><creator>Kamata, Kenichi</creator><creator>Park, Sam-Yong</creator><creator>Tamura, Koji</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope></search><sort><creationdate>20211020</creationdate><title>Crystal structure of Nanoarchaeum equitans tyrosyl-tRNA synthetase and its aminoacylation activity toward tRNA Tyr with an extra guanosine residue at the 5'-terminus</title><author>Horikoshi, Tatsuya ; Noguchi, Hiroki ; Umehara, Takuya ; Mutsuro-Aoki, Hiromi ; Kurihara, Ryodai ; Noguchi, Ryohei ; Hashimoto, Takahiro ; Watanabe, Yuki ; Ando, Tadashi ; Kamata, Kenichi ; Park, Sam-Yong ; Tamura, Koji</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-pubmed_primary_344614413</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Aminoacylation</topic><topic>Archaeal Proteins - chemistry</topic><topic>Archaeal Proteins - genetics</topic><topic>Archaeal Proteins - metabolism</topic><topic>Crystallography, X-Ray - methods</topic><topic>Guanosine - chemistry</topic><topic>Models, Molecular</topic><topic>Nanoarchaeota - enzymology</topic><topic>Protein Structural Elements</topic><topic>RNA, Transfer, Tyr - chemistry</topic><topic>RNA, Transfer, Tyr - genetics</topic><topic>RNA, Transfer, Tyr - metabolism</topic><topic>Tyrosine-tRNA Ligase - chemistry</topic><topic>Tyrosine-tRNA Ligase - genetics</topic><topic>Tyrosine-tRNA Ligase - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Horikoshi, Tatsuya</creatorcontrib><creatorcontrib>Noguchi, Hiroki</creatorcontrib><creatorcontrib>Umehara, Takuya</creatorcontrib><creatorcontrib>Mutsuro-Aoki, Hiromi</creatorcontrib><creatorcontrib>Kurihara, Ryodai</creatorcontrib><creatorcontrib>Noguchi, Ryohei</creatorcontrib><creatorcontrib>Hashimoto, Takahiro</creatorcontrib><creatorcontrib>Watanabe, Yuki</creatorcontrib><creatorcontrib>Ando, Tadashi</creatorcontrib><creatorcontrib>Kamata, Kenichi</creatorcontrib><creatorcontrib>Park, Sam-Yong</creatorcontrib><creatorcontrib>Tamura, Koji</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Horikoshi, Tatsuya</au><au>Noguchi, Hiroki</au><au>Umehara, Takuya</au><au>Mutsuro-Aoki, Hiromi</au><au>Kurihara, Ryodai</au><au>Noguchi, Ryohei</au><au>Hashimoto, Takahiro</au><au>Watanabe, Yuki</au><au>Ando, Tadashi</au><au>Kamata, Kenichi</au><au>Park, Sam-Yong</au><au>Tamura, Koji</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal structure of Nanoarchaeum equitans tyrosyl-tRNA synthetase and its aminoacylation activity toward tRNA Tyr with an extra guanosine residue at the 5'-terminus</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2021-10-20</date><risdate>2021</risdate><volume>575</volume><spage>90</spage><pages>90-</pages><eissn>1090-2104</eissn><abstract>tRNA
of Nanoarchaeum equitans has a remarkable feature with an extra guanosine residue at the 5'-terminus. However, the N. equitans tRNA
mutant without extra guanosine at the 5'-end was tyrosylated by tyrosyl-tRNA synthase (TyrRS). We solved the crystal structure of N. equitans TyrRS at 2.80 Å resolution. By comparing the present solved structure with the complex structures TyrRS with tRNA
of Thermus thermophilus and Methanocaldococcus jannaschii, an arginine substitution mutant of N. equitans TyrRS at Ile200 (I200R), which is the putative closest candidate to the 5'-phosphate of C1 of N. equitans tRNA
, was prepared. The I200R mutant tyrosylated not only wild-type tRNA
but also the tRNA without the G-1 residue. Further tyrosylation analysis revealed that the second base of the anticodon (U35), discriminator base (A73), and C1:G72 base pair are strong recognition sites.</abstract><cop>United States</cop><pmid>34461441</pmid></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 2021-10, Vol.575, p.90 |
| issn | 1090-2104 |
| language | eng |
| recordid | cdi_pubmed_primary_34461441 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Aminoacylation Archaeal Proteins - chemistry Archaeal Proteins - genetics Archaeal Proteins - metabolism Crystallography, X-Ray - methods Guanosine - chemistry Models, Molecular Nanoarchaeota - enzymology Protein Structural Elements RNA, Transfer, Tyr - chemistry RNA, Transfer, Tyr - genetics RNA, Transfer, Tyr - metabolism Tyrosine-tRNA Ligase - chemistry Tyrosine-tRNA Ligase - genetics Tyrosine-tRNA Ligase - metabolism |
| title | Crystal structure of Nanoarchaeum equitans tyrosyl-tRNA synthetase and its aminoacylation activity toward tRNA Tyr with an extra guanosine residue at the 5'-terminus |
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