Solution X‐ray scattering highlights discrepancies in Plasmodium multi‐aminoacyl‐tRNA synthetase complexes
tRip is a tRNA import protein specific to Plasmodium, the causative agent of malaria. In addition to its membrane localization and tRNA trafficking properties, tRip has the capacity to associate with three aminoacyl‐tRNA synthetases (aaRS), the glutamyl‐ (ERS), glutaminyl‐ (QRS), and methionyl‐ (MRS...
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| Veröffentlicht in: | Protein science 2023-02, Vol.32 (2), p.e4564-n/a |
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| description | tRip is a tRNA import protein specific to Plasmodium, the causative agent of malaria. In addition to its membrane localization and tRNA trafficking properties, tRip has the capacity to associate with three aminoacyl‐tRNA synthetases (aaRS), the glutamyl‐ (ERS), glutaminyl‐ (QRS), and methionyl‐ (MRS) tRNA synthetases. In eukaryotes, such multi‐aaRSs complexes (MSC) regulate the moonlighting activities of aaRSs. In Plasmodium, tRip and the three aaRSs all contain an N‐terminal GST‐like domain involved in the assembly of two independent complexes: the Q‐complex (tRip:ERS:QRS) and the M‐complex (tRip:ERS:MRS) with a 2:2:2 stoichiometry and in which the association of the GST‐like domains of tRip and ERS (tRip‐N:ERS‐N) is central. In this study, the crystal structure of the N‐terminal GST‐like domain of ERS was solved and made possible further investigation of the solution architecture of the Q‐ and M‐complexes by small‐angle x‐ray scattering (SAXS). This strategy relied on the engineering of a tRip‐N‐ERS‐N chimeric protein to study the structural scaffold of both Plasmodium MSCs and confirm the unique homodimerization pattern of tRip in solution. The biological impact of these structural arrangements is discussed.
PDB Code(s): 8BCQ and 8BHD |
| doi_str_mv | 10.1002/pro.4564 |
| format | Article |
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PDB Code(s): 8BCQ and 8BHD</description><identifier>ISSN: 0961-8368</identifier><identifier>EISSN: 1469-896X</identifier><identifier>DOI: 10.1002/pro.4564</identifier><identifier>PMID: 36606712</identifier><language>eng</language><publisher>Hoboken, USA: John Wiley & Sons, Inc</publisher><subject>Amino Acyl-tRNA Synthetases - chemistry ; aminoacyl‐ synthetase‐interacting multifunctional proteins (AIMP) ; aminoacyl‐tRNA synthetase ; Biochemistry, Molecular Biology ; Crystal structure ; Domains ; Eukaryotes ; Full‐length Paper ; Full‐length Papers ; GST‐like domain ; Life Sciences ; Localization ; Malaria ; Membrane trafficking ; Microbiology and Parasitology ; multi‐aminoacyl‐tRNA synthetase complex (MARS/MSC) ; Parasitology ; Plasmodium ; protein complex ; Protein transport ; Proteins ; Reagents ; RNA binding protein ; RNA, Transfer ; Scattering ; Scattering, Small Angle ; Stoichiometry ; Structural Biology ; Transfer RNA ; tRip ; tRNA ; Vector-borne diseases ; X-Ray Diffraction ; X-Rays</subject><ispartof>Protein science, 2023-02, Vol.32 (2), p.e4564-n/a</ispartof><rights>2023 The Authors. published by Wiley Periodicals LLC on behalf of The Protein Society.</rights><rights>2023 The Authors. Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society.</rights><rights>2023. This article is published under http://creativecommons.org/licenses/by-nc-nd/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>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4384-692fdb2a1d962ab1d28d16596fdfddf266acc5b9772e9fe2b84f7f41ca7de9223</citedby><cites>FETCH-LOGICAL-c4384-692fdb2a1d962ab1d28d16596fdfddf266acc5b9772e9fe2b84f7f41ca7de9223</cites><orcidid>0000-0002-8079-5303 ; 0000-0002-8766-287X</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/PMC9878616/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9878616/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,1433,27923,27924,45573,45574,46408,46832,53790,53792</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/36606712$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-03938857$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Jaramillo Ponce, José R.</creatorcontrib><creatorcontrib>Théobald‐Dietrich, Anne</creatorcontrib><creatorcontrib>Bénas, Philippe</creatorcontrib><creatorcontrib>Paulus, Caroline</creatorcontrib><creatorcontrib>Sauter, Claude</creatorcontrib><creatorcontrib>Frugier, Magali</creatorcontrib><title>Solution X‐ray scattering highlights discrepancies in Plasmodium multi‐aminoacyl‐tRNA synthetase complexes</title><title>Protein science</title><addtitle>Protein Sci</addtitle><description>tRip is a tRNA import protein specific to Plasmodium, the causative agent of malaria. In addition to its membrane localization and tRNA trafficking properties, tRip has the capacity to associate with three aminoacyl‐tRNA synthetases (aaRS), the glutamyl‐ (ERS), glutaminyl‐ (QRS), and methionyl‐ (MRS) tRNA synthetases. In eukaryotes, such multi‐aaRSs complexes (MSC) regulate the moonlighting activities of aaRSs. In Plasmodium, tRip and the three aaRSs all contain an N‐terminal GST‐like domain involved in the assembly of two independent complexes: the Q‐complex (tRip:ERS:QRS) and the M‐complex (tRip:ERS:MRS) with a 2:2:2 stoichiometry and in which the association of the GST‐like domains of tRip and ERS (tRip‐N:ERS‐N) is central. In this study, the crystal structure of the N‐terminal GST‐like domain of ERS was solved and made possible further investigation of the solution architecture of the Q‐ and M‐complexes by small‐angle x‐ray scattering (SAXS). This strategy relied on the engineering of a tRip‐N‐ERS‐N chimeric protein to study the structural scaffold of both Plasmodium MSCs and confirm the unique homodimerization pattern of tRip in solution. The biological impact of these structural arrangements is discussed.
PDB Code(s): 8BCQ and 8BHD</description><subject>Amino Acyl-tRNA Synthetases - chemistry</subject><subject>aminoacyl‐ synthetase‐interacting multifunctional proteins (AIMP)</subject><subject>aminoacyl‐tRNA synthetase</subject><subject>Biochemistry, Molecular Biology</subject><subject>Crystal structure</subject><subject>Domains</subject><subject>Eukaryotes</subject><subject>Full‐length Paper</subject><subject>Full‐length Papers</subject><subject>GST‐like domain</subject><subject>Life Sciences</subject><subject>Localization</subject><subject>Malaria</subject><subject>Membrane trafficking</subject><subject>Microbiology and Parasitology</subject><subject>multi‐aminoacyl‐tRNA synthetase complex (MARS/MSC)</subject><subject>Parasitology</subject><subject>Plasmodium</subject><subject>protein complex</subject><subject>Protein transport</subject><subject>Proteins</subject><subject>Reagents</subject><subject>RNA binding protein</subject><subject>RNA, Transfer</subject><subject>Scattering</subject><subject>Scattering, Small Angle</subject><subject>Stoichiometry</subject><subject>Structural Biology</subject><subject>Transfer RNA</subject><subject>tRip</subject><subject>tRNA</subject><subject>Vector-borne diseases</subject><subject>X-Ray Diffraction</subject><subject>X-Rays</subject><issn>0961-8368</issn><issn>1469-896X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><sourceid>WIN</sourceid><sourceid>EIF</sourceid><recordid>eNp1kc1uFSEUgInR2Gs18QnMJG50MRWYGQY2JjeNWpMb21RNuiMMMHdoGJgCU52dj-Az-iRyvbVqExeEv-98B84B4CmCRwhC_GoK_qhuSH0PrFBNWEkZubgPVpARVNKK0APwKMZLCGGNcPUQHFSEQNIivALTR2_nZLwrLn58-x7EUkQpUtLBuG0xmO1g80ixUCbKoCfhpNGxMK44syKOXpl5LMbZJpOjxWicF3KxeZ3OP6yLuLg06CSiLqQfJ6u_6vgYPOiFjfrJzXwIPr998-n4pNycvnt_vN6Usq5oXRKGe9VhgRQjWHRIYaoQaRjpVa9UjwkRUjYda1usWa9xR-u-7WskRas0w7g6BK_33mnuRq2kdikIy6dgRhEW7oXh_944M_Ctv-aMtpQgkgUv94LhTtjJesN3Z7BiFaVNe71L9uImWfBXs46Jj7le2lrhtJ8jxy1BjJKmoRl9fge99HNwuRSZaiFBmFXVH6EMPsag-9sXIMh3Lc97z3ctz-izvz96C_7ucQbKPfDFWL38V8TPzk9_CX8ChvG7ew</recordid><startdate>202302</startdate><enddate>202302</enddate><creator>Jaramillo Ponce, José R.</creator><creator>Théobald‐Dietrich, Anne</creator><creator>Bénas, Philippe</creator><creator>Paulus, Caroline</creator><creator>Sauter, Claude</creator><creator>Frugier, Magali</creator><general>John Wiley & Sons, Inc</general><general>Wiley Subscription Services, Inc</general><general>Wiley</general><scope>24P</scope><scope>WIN</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>7QO</scope><scope>7T5</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>1XC</scope><scope>VOOES</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-8079-5303</orcidid><orcidid>https://orcid.org/0000-0002-8766-287X</orcidid></search><sort><creationdate>202302</creationdate><title>Solution X‐ray scattering highlights discrepancies in Plasmodium multi‐aminoacyl‐tRNA synthetase complexes</title><author>Jaramillo Ponce, José R. ; Théobald‐Dietrich, Anne ; Bénas, Philippe ; Paulus, Caroline ; Sauter, Claude ; Frugier, Magali</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4384-692fdb2a1d962ab1d28d16596fdfddf266acc5b9772e9fe2b84f7f41ca7de9223</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Amino Acyl-tRNA Synthetases - chemistry</topic><topic>aminoacyl‐ synthetase‐interacting multifunctional proteins (AIMP)</topic><topic>aminoacyl‐tRNA synthetase</topic><topic>Biochemistry, Molecular Biology</topic><topic>Crystal structure</topic><topic>Domains</topic><topic>Eukaryotes</topic><topic>Full‐length Paper</topic><topic>Full‐length Papers</topic><topic>GST‐like domain</topic><topic>Life Sciences</topic><topic>Localization</topic><topic>Malaria</topic><topic>Membrane trafficking</topic><topic>Microbiology and Parasitology</topic><topic>multi‐aminoacyl‐tRNA synthetase complex (MARS/MSC)</topic><topic>Parasitology</topic><topic>Plasmodium</topic><topic>protein complex</topic><topic>Protein transport</topic><topic>Proteins</topic><topic>Reagents</topic><topic>RNA binding protein</topic><topic>RNA, Transfer</topic><topic>Scattering</topic><topic>Scattering, Small Angle</topic><topic>Stoichiometry</topic><topic>Structural Biology</topic><topic>Transfer RNA</topic><topic>tRip</topic><topic>tRNA</topic><topic>Vector-borne diseases</topic><topic>X-Ray Diffraction</topic><topic>X-Rays</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jaramillo Ponce, José R.</creatorcontrib><creatorcontrib>Théobald‐Dietrich, Anne</creatorcontrib><creatorcontrib>Bénas, Philippe</creatorcontrib><creatorcontrib>Paulus, Caroline</creatorcontrib><creatorcontrib>Sauter, Claude</creatorcontrib><creatorcontrib>Frugier, Magali</creatorcontrib><collection>Wiley-Blackwell Open Access Titles</collection><collection>Wiley Free Content</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Immunology Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>Hyper Article en Ligne (HAL) (Open Access)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Protein science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jaramillo Ponce, José R.</au><au>Théobald‐Dietrich, Anne</au><au>Bénas, Philippe</au><au>Paulus, Caroline</au><au>Sauter, Claude</au><au>Frugier, Magali</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Solution X‐ray scattering highlights discrepancies in Plasmodium multi‐aminoacyl‐tRNA synthetase complexes</atitle><jtitle>Protein science</jtitle><addtitle>Protein Sci</addtitle><date>2023-02</date><risdate>2023</risdate><volume>32</volume><issue>2</issue><spage>e4564</spage><epage>n/a</epage><pages>e4564-n/a</pages><issn>0961-8368</issn><eissn>1469-896X</eissn><abstract>tRip is a tRNA import protein specific to Plasmodium, the causative agent of malaria. In addition to its membrane localization and tRNA trafficking properties, tRip has the capacity to associate with three aminoacyl‐tRNA synthetases (aaRS), the glutamyl‐ (ERS), glutaminyl‐ (QRS), and methionyl‐ (MRS) tRNA synthetases. In eukaryotes, such multi‐aaRSs complexes (MSC) regulate the moonlighting activities of aaRSs. In Plasmodium, tRip and the three aaRSs all contain an N‐terminal GST‐like domain involved in the assembly of two independent complexes: the Q‐complex (tRip:ERS:QRS) and the M‐complex (tRip:ERS:MRS) with a 2:2:2 stoichiometry and in which the association of the GST‐like domains of tRip and ERS (tRip‐N:ERS‐N) is central. In this study, the crystal structure of the N‐terminal GST‐like domain of ERS was solved and made possible further investigation of the solution architecture of the Q‐ and M‐complexes by small‐angle x‐ray scattering (SAXS). This strategy relied on the engineering of a tRip‐N‐ERS‐N chimeric protein to study the structural scaffold of both Plasmodium MSCs and confirm the unique homodimerization pattern of tRip in solution. The biological impact of these structural arrangements is discussed.
PDB Code(s): 8BCQ and 8BHD</abstract><cop>Hoboken, USA</cop><pub>John Wiley & Sons, Inc</pub><pmid>36606712</pmid><doi>10.1002/pro.4564</doi><tpages>18</tpages><orcidid>https://orcid.org/0000-0002-8079-5303</orcidid><orcidid>https://orcid.org/0000-0002-8766-287X</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acyl-tRNA Synthetases - chemistry aminoacyl‐ synthetase‐interacting multifunctional proteins (AIMP) aminoacyl‐tRNA synthetase Biochemistry, Molecular Biology Crystal structure Domains Eukaryotes Full‐length Paper Full‐length Papers GST‐like domain Life Sciences Localization Malaria Membrane trafficking Microbiology and Parasitology multi‐aminoacyl‐tRNA synthetase complex (MARS/MSC) Parasitology Plasmodium protein complex Protein transport Proteins Reagents RNA binding protein RNA, Transfer Scattering Scattering, Small Angle Stoichiometry Structural Biology Transfer RNA tRip tRNA Vector-borne diseases X-Ray Diffraction X-Rays |
| title | Solution X‐ray scattering highlights discrepancies in Plasmodium multi‐aminoacyl‐tRNA synthetase complexes |
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