Effects of engineering complementary charged residues into the hydrophobic subunit interface of tyrosyl-tRNA synthetase

Effects of engineering complementary charged residues into the hydrophobic subunit interface of tyrosyl-tRNA synthetase

Wild-type tyrosyl-tRNA synthetase (TyrTS) from Bacillus stearothermophilus is a symmetrical dimer. Four different heterodimeric enzymes have been produced by site-directed mutagenesis at the subunit interface so that the monomers are linked by a potential salt bridge in a hydrophobic environment. Th...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Biochemistry (Easton) 1987-06, Vol.26 (13), p.4131-4138
Hauptverfasser: Ward, Walter H. J., Jones, D. Hugh, Fersht, Alan R.
Format: Artikel
Sprache:eng
Schlagworte:
Bacillus stearothermophilus
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 4138
container_issue 13
container_start_page 4131
container_title Biochemistry (Easton)
container_volume 26
creator Ward, Walter H. J.
Jones, D. Hugh
Fersht, Alan R.
description Wild-type tyrosyl-tRNA synthetase (TyrTS) from Bacillus stearothermophilus is a symmetrical dimer. Four different heterodimeric enzymes have been produced by site-directed mutagenesis at the subunit interface so that the monomers are linked by a potential salt bridge in a hydrophobic environment. The two Phe-164 residues of wild-type TyrTS are on the axis of symmetry and interact in hydrophobic region of the subunit interface. Mutation of Phe-164 to aspartate or glutamate in full-length TyrTS and to lysine or arginine in an active truncated enzyme ( Delta TyrTS) induces reversible dissociation of the enzyme into inactive monomers.
doi_str_mv 10.1021/bi00387a058
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_14893479</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>14893479</sourcerecordid><originalsourceid>FETCH-LOGICAL-a247t-8b47d70858b42bb61e6f03eab3e422bf87652a9597d02d4ce7468db1b71f45093</originalsourceid><addsrcrecordid>eNptkE9P3DAQxS3USiyUE1_AJzigtLbjxMkRUQpVaYv4c-Fi2c5415C1t7Yjmm-PV1tVPfQ0M5rfPM17CB1T8pESRj9pR0jdCUWabg8taMNIxfu-eYcWhJC2Yn1L9tFBSs9l5ETwBXq9tBZMTjhYDH7pPEB0folNWG9GWIPPKs7YrFRcwoAjJDdMkLDzOeC8Aryahxg2q6CdwWnSk3d5u4RolYGtaJ5jSPNY5bsf5zjNvhxlleADem_VmODoTz1Ej18uHy6uq5ufV18vzm8qxbjIVae5GATpmtIwrVsKrSU1KF0DZ0zbTrQNU33Ti4GwgRsQvO0GTbWgljekrw_RyU53E8Ov8nmWa5cMjKPyEKYkKe_6mosteLYDTfk3RbByE926mJeUyG248p9wC13taJcy_P6LqvgiW1GLRj7c3sunz-Ib_95dy9vCn-54ZZJ8DlP0xfR_ld8AbSaKjw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>14893479</pqid></control><display><type>article</type><title>Effects of engineering complementary charged residues into the hydrophobic subunit interface of tyrosyl-tRNA synthetase</title><source>ACS Publications</source><creator>Ward, Walter H. J. ; Jones, D. Hugh ; Fersht, Alan R.</creator><creatorcontrib>Ward, Walter H. J. ; Jones, D. Hugh ; Fersht, Alan R.</creatorcontrib><description>Wild-type tyrosyl-tRNA synthetase (TyrTS) from Bacillus stearothermophilus is a symmetrical dimer. Four different heterodimeric enzymes have been produced by site-directed mutagenesis at the subunit interface so that the monomers are linked by a potential salt bridge in a hydrophobic environment. The two Phe-164 residues of wild-type TyrTS are on the axis of symmetry and interact in hydrophobic region of the subunit interface. Mutation of Phe-164 to aspartate or glutamate in full-length TyrTS and to lysine or arginine in an active truncated enzyme ( Delta TyrTS) induces reversible dissociation of the enzyme into inactive monomers.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00387a058</identifier><language>eng</language><publisher>American Chemical Society</publisher><subject>Bacillus stearothermophilus</subject><ispartof>Biochemistry (Easton), 1987-06, Vol.26 (13), p.4131-4138</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a247t-8b47d70858b42bb61e6f03eab3e422bf87652a9597d02d4ce7468db1b71f45093</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00387a058$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00387a058$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27053,27901,27902,56713,56763</link.rule.ids></links><search><creatorcontrib>Ward, Walter H. J.</creatorcontrib><creatorcontrib>Jones, D. Hugh</creatorcontrib><creatorcontrib>Fersht, Alan R.</creatorcontrib><title>Effects of engineering complementary charged residues into the hydrophobic subunit interface of tyrosyl-tRNA synthetase</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>Wild-type tyrosyl-tRNA synthetase (TyrTS) from Bacillus stearothermophilus is a symmetrical dimer. Four different heterodimeric enzymes have been produced by site-directed mutagenesis at the subunit interface so that the monomers are linked by a potential salt bridge in a hydrophobic environment. The two Phe-164 residues of wild-type TyrTS are on the axis of symmetry and interact in hydrophobic region of the subunit interface. Mutation of Phe-164 to aspartate or glutamate in full-length TyrTS and to lysine or arginine in an active truncated enzyme ( Delta TyrTS) induces reversible dissociation of the enzyme into inactive monomers.</description><subject>Bacillus stearothermophilus</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><recordid>eNptkE9P3DAQxS3USiyUE1_AJzigtLbjxMkRUQpVaYv4c-Fi2c5415C1t7Yjmm-PV1tVPfQ0M5rfPM17CB1T8pESRj9pR0jdCUWabg8taMNIxfu-eYcWhJC2Yn1L9tFBSs9l5ETwBXq9tBZMTjhYDH7pPEB0folNWG9GWIPPKs7YrFRcwoAjJDdMkLDzOeC8Aryahxg2q6CdwWnSk3d5u4RolYGtaJ5jSPNY5bsf5zjNvhxlleADem_VmODoTz1Ej18uHy6uq5ufV18vzm8qxbjIVae5GATpmtIwrVsKrSU1KF0DZ0zbTrQNU33Ti4GwgRsQvO0GTbWgljekrw_RyU53E8Ov8nmWa5cMjKPyEKYkKe_6mosteLYDTfk3RbByE926mJeUyG248p9wC13taJcy_P6LqvgiW1GLRj7c3sunz-Ib_95dy9vCn-54ZZJ8DlP0xfR_ld8AbSaKjw</recordid><startdate>19870601</startdate><enddate>19870601</enddate><creator>Ward, Walter H. J.</creator><creator>Jones, D. Hugh</creator><creator>Fersht, Alan R.</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope></search><sort><creationdate>19870601</creationdate><title>Effects of engineering complementary charged residues into the hydrophobic subunit interface of tyrosyl-tRNA synthetase</title><author>Ward, Walter H. J. ; Jones, D. Hugh ; Fersht, Alan R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a247t-8b47d70858b42bb61e6f03eab3e422bf87652a9597d02d4ce7468db1b71f45093</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Bacillus stearothermophilus</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ward, Walter H. J.</creatorcontrib><creatorcontrib>Jones, D. Hugh</creatorcontrib><creatorcontrib>Fersht, Alan R.</creatorcontrib><collection>Istex</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ward, Walter H. J.</au><au>Jones, D. Hugh</au><au>Fersht, Alan R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effects of engineering complementary charged residues into the hydrophobic subunit interface of tyrosyl-tRNA synthetase</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1987-06-01</date><risdate>1987</risdate><volume>26</volume><issue>13</issue><spage>4131</spage><epage>4138</epage><pages>4131-4138</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>Wild-type tyrosyl-tRNA synthetase (TyrTS) from Bacillus stearothermophilus is a symmetrical dimer. Four different heterodimeric enzymes have been produced by site-directed mutagenesis at the subunit interface so that the monomers are linked by a potential salt bridge in a hydrophobic environment. The two Phe-164 residues of wild-type TyrTS are on the axis of symmetry and interact in hydrophobic region of the subunit interface. Mutation of Phe-164 to aspartate or glutamate in full-length TyrTS and to lysine or arginine in an active truncated enzyme ( Delta TyrTS) induces reversible dissociation of the enzyme into inactive monomers.</abstract><pub>American Chemical Society</pub><doi>10.1021/bi00387a058</doi><tpages>8</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0006-2960
ispartof Biochemistry (Easton), 1987-06, Vol.26 (13), p.4131-4138
issn 0006-2960
1520-4995
language eng
recordid cdi_proquest_miscellaneous_14893479
source ACS Publications
subjects Bacillus stearothermophilus
title Effects of engineering complementary charged residues into the hydrophobic subunit interface of tyrosyl-tRNA synthetase
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-02T10%3A15%3A30IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Effects%20of%20engineering%20complementary%20charged%20residues%20into%20the%20hydrophobic%20subunit%20interface%20of%20tyrosyl-tRNA%20synthetase&rft.jtitle=Biochemistry%20(Easton)&rft.au=Ward,%20Walter%20H.%20J.&rft.date=1987-06-01&rft.volume=26&rft.issue=13&rft.spage=4131&rft.epage=4138&rft.pages=4131-4138&rft.issn=0006-2960&rft.eissn=1520-4995&rft_id=info:doi/10.1021/bi00387a058&rft_dat=%3Cproquest_cross%3E14893479%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=14893479&rft_id=info:pmid/&rfr_iscdi=true