Structural Analysis of the Rubisco-Assembly Chaperone RbcX-II from Chlamydomonas reinhardtii
The most prevalent form of the Rubisco enzyme is a complex of eight catalytic large subunits (RbcL) and eight regulatory small subunits (RbcS). Rubisco biogenesis depends on the assistance by specific molecular chaperones. The assembly chaperone RbcX stabilizes the RbcL subunits after folding by cha...
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| description | The most prevalent form of the Rubisco enzyme is a complex of eight catalytic large subunits (RbcL) and eight regulatory small subunits (RbcS). Rubisco biogenesis depends on the assistance by specific molecular chaperones. The assembly chaperone RbcX stabilizes the RbcL subunits after folding by chaperonin and mediates their assembly to the RbcL8 core complex, from which RbcX is displaced by RbcS to form active holoenzyme. Two isoforms of RbcX are found in eukaryotes, RbcX-I, which is more closely related to cyanobacterial RbcX, and the more distant RbcX-II. The green algae Chlamydomonas reinhardtii contains only RbcX-II isoforms, CrRbcX-IIa and CrRbcX-IIb. Here we solved the crystal structure of CrRbcX-IIa and show that it forms an arc-shaped dimer with a central hydrophobic cleft for binding the C-terminal sequence of RbcL. Like other RbcX proteins, CrRbcX-IIa supports the assembly of cyanobacterial Rubisco in vitro, albeit with reduced activity relative to cyanobacterial RbcX-I. Structural analysis of a fusion protein of CrRbcX-IIa and the C-terminal peptide of RbcL suggests that the peptide binding mode of RbcX-II may differ from that of cyanobacterial RbcX. RbcX homologs appear to have adapted to their cognate Rubisco clients as a result of co-evolution. |
| doi_str_mv | 10.1371/journal.pone.0135448 |
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Rubisco biogenesis depends on the assistance by specific molecular chaperones. The assembly chaperone RbcX stabilizes the RbcL subunits after folding by chaperonin and mediates their assembly to the RbcL8 core complex, from which RbcX is displaced by RbcS to form active holoenzyme. Two isoforms of RbcX are found in eukaryotes, RbcX-I, which is more closely related to cyanobacterial RbcX, and the more distant RbcX-II. The green algae Chlamydomonas reinhardtii contains only RbcX-II isoforms, CrRbcX-IIa and CrRbcX-IIb. Here we solved the crystal structure of CrRbcX-IIa and show that it forms an arc-shaped dimer with a central hydrophobic cleft for binding the C-terminal sequence of RbcL. Like other RbcX proteins, CrRbcX-IIa supports the assembly of cyanobacterial Rubisco in vitro, albeit with reduced activity relative to cyanobacterial RbcX-I. Structural analysis of a fusion protein of CrRbcX-IIa and the C-terminal peptide of RbcL suggests that the peptide binding mode of RbcX-II may differ from that of cyanobacterial RbcX. RbcX homologs appear to have adapted to their cognate Rubisco clients as a result of co-evolution.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0135448</identifier><identifier>PMID: 26305355</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Algae ; Amino Acid Sequence ; Assembly ; Bacterial Proteins - chemistry ; Binding ; Binding Sites ; Biochemistry ; Biosynthesis ; Catalysis ; Chaperones ; Chlamydomonas reinhardtii ; Chlamydomonas reinhardtii - chemistry ; Chlorophyta ; Chloroplasts ; Crystal structure ; Crystallography ; Crystallography, X-Ray ; Cyanobacteria ; E coli ; Escherichia coli ; Eukaryotes ; Fusion protein ; Homology ; Hydrophobicity ; Isoforms ; Molecular chains ; Molecular Chaperones - chemistry ; Molecular structure ; Multiprotein Complexes - chemistry ; Peptides ; Plasmids ; Protein Binding ; Protein Conformation ; Protein Folding ; Proteins ; Ribulose-bisphosphate carboxylase ; Ribulose-Bisphosphate Carboxylase - chemistry ; Structural analysis ; Synechococcus ; Synechococcus elongatus</subject><ispartof>PloS one, 2015-08, Vol.10 (8), p.e0135448-e0135448</ispartof><rights>2015 Bracher et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2015 Bracher et al 2015 Bracher et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c526t-1caa4c7d3fc3f6c47c21241daf56269cad0f9a8fdd3e5b34d11f3420960c038c3</citedby><cites>FETCH-LOGICAL-c526t-1caa4c7d3fc3f6c47c21241daf56269cad0f9a8fdd3e5b34d11f3420960c038c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4549274/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4549274/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79343,79344</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26305355$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bracher, Andreas</creatorcontrib><creatorcontrib>Hauser, Thomas</creatorcontrib><creatorcontrib>Liu, Cuimin</creatorcontrib><creatorcontrib>Hartl, F Ulrich</creatorcontrib><creatorcontrib>Hayer-Hartl, Manajit</creatorcontrib><title>Structural Analysis of the Rubisco-Assembly Chaperone RbcX-II from Chlamydomonas reinhardtii</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>The most prevalent form of the Rubisco enzyme is a complex of eight catalytic large subunits (RbcL) and eight regulatory small subunits (RbcS). Rubisco biogenesis depends on the assistance by specific molecular chaperones. The assembly chaperone RbcX stabilizes the RbcL subunits after folding by chaperonin and mediates their assembly to the RbcL8 core complex, from which RbcX is displaced by RbcS to form active holoenzyme. Two isoforms of RbcX are found in eukaryotes, RbcX-I, which is more closely related to cyanobacterial RbcX, and the more distant RbcX-II. The green algae Chlamydomonas reinhardtii contains only RbcX-II isoforms, CrRbcX-IIa and CrRbcX-IIb. Here we solved the crystal structure of CrRbcX-IIa and show that it forms an arc-shaped dimer with a central hydrophobic cleft for binding the C-terminal sequence of RbcL. Like other RbcX proteins, CrRbcX-IIa supports the assembly of cyanobacterial Rubisco in vitro, albeit with reduced activity relative to cyanobacterial RbcX-I. Structural analysis of a fusion protein of CrRbcX-IIa and the C-terminal peptide of RbcL suggests that the peptide binding mode of RbcX-II may differ from that of cyanobacterial RbcX. RbcX homologs appear to have adapted to their cognate Rubisco clients as a result of co-evolution.</description><subject>Algae</subject><subject>Amino Acid Sequence</subject><subject>Assembly</subject><subject>Bacterial Proteins - chemistry</subject><subject>Binding</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biosynthesis</subject><subject>Catalysis</subject><subject>Chaperones</subject><subject>Chlamydomonas reinhardtii</subject><subject>Chlamydomonas reinhardtii - chemistry</subject><subject>Chlorophyta</subject><subject>Chloroplasts</subject><subject>Crystal structure</subject><subject>Crystallography</subject><subject>Crystallography, X-Ray</subject><subject>Cyanobacteria</subject><subject>E coli</subject><subject>Escherichia coli</subject><subject>Eukaryotes</subject><subject>Fusion protein</subject><subject>Homology</subject><subject>Hydrophobicity</subject><subject>Isoforms</subject><subject>Molecular chains</subject><subject>Molecular Chaperones - chemistry</subject><subject>Molecular structure</subject><subject>Multiprotein Complexes - chemistry</subject><subject>Peptides</subject><subject>Plasmids</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Protein Folding</subject><subject>Proteins</subject><subject>Ribulose-bisphosphate carboxylase</subject><subject>Ribulose-Bisphosphate Carboxylase - chemistry</subject><subject>Structural analysis</subject><subject>Synechococcus</subject><subject>Synechococcus elongatus</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><sourceid>DOA</sourceid><recordid>eNptUttq3DAQNaWlSZP8QWkNeemLt7pbfiksSy8LgUKaQh8CQpZGWS22tZXswv59tVknJKUg0DBz5szM4RTFW4wWmNb44zZMcdDdYhcGWCBMOWPyRXGKG0oqQRB9-SQ-Kd6ktEWIUynE6-KECJpjzk-L2x9jnMw4Rd2Vy0y3Tz6VwZXjBsrrqfXJhGqZEvRtty9XG72DmOeV1635Va3XpYuhz-lO93sb-jDoVEbww0ZHO3p_XrxyuktwMf9nxc8vn29W36qr71_Xq-VVZTgRY4WN1szUljpDnTCsNgQThq12XBDRGG2Ra7R01lLgLWUWY0cZQY1ABlFp6Fnx_si760JSszBJ4RpJJkkteEasjwgb9Fbtou913KugvbpPhHindBy96UBJhKUBoPkxRmzTgqNNAxzAYC3hwPVpnja1PVgDw5jVe0b6vDL4jboLfxTjrCE1ywQfZoIYfk-QRtVnnaHr9ABhut-75lwwIjP08h_o_69jR5SJIaUI7nEZjNTBLA9d6mAWNZslt717eshj04M76F_Pdr7v</recordid><startdate>20150825</startdate><enddate>20150825</enddate><creator>Bracher, Andreas</creator><creator>Hauser, Thomas</creator><creator>Liu, Cuimin</creator><creator>Hartl, F Ulrich</creator><creator>Hayer-Hartl, Manajit</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><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>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20150825</creationdate><title>Structural Analysis of the Rubisco-Assembly Chaperone RbcX-II from Chlamydomonas reinhardtii</title><author>Bracher, Andreas ; Hauser, Thomas ; Liu, Cuimin ; Hartl, F Ulrich ; Hayer-Hartl, Manajit</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c526t-1caa4c7d3fc3f6c47c21241daf56269cad0f9a8fdd3e5b34d11f3420960c038c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Algae</topic><topic>Amino Acid Sequence</topic><topic>Assembly</topic><topic>Bacterial Proteins - chemistry</topic><topic>Binding</topic><topic>Binding Sites</topic><topic>Biochemistry</topic><topic>Biosynthesis</topic><topic>Catalysis</topic><topic>Chaperones</topic><topic>Chlamydomonas reinhardtii</topic><topic>Chlamydomonas reinhardtii - chemistry</topic><topic>Chlorophyta</topic><topic>Chloroplasts</topic><topic>Crystal structure</topic><topic>Crystallography</topic><topic>Crystallography, X-Ray</topic><topic>Cyanobacteria</topic><topic>E coli</topic><topic>Escherichia coli</topic><topic>Eukaryotes</topic><topic>Fusion protein</topic><topic>Homology</topic><topic>Hydrophobicity</topic><topic>Isoforms</topic><topic>Molecular chains</topic><topic>Molecular Chaperones - chemistry</topic><topic>Molecular structure</topic><topic>Multiprotein Complexes - chemistry</topic><topic>Peptides</topic><topic>Plasmids</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Protein Folding</topic><topic>Proteins</topic><topic>Ribulose-bisphosphate carboxylase</topic><topic>Ribulose-Bisphosphate Carboxylase - chemistry</topic><topic>Structural analysis</topic><topic>Synechococcus</topic><topic>Synechococcus elongatus</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bracher, Andreas</creatorcontrib><creatorcontrib>Hauser, Thomas</creatorcontrib><creatorcontrib>Liu, Cuimin</creatorcontrib><creatorcontrib>Hartl, F Ulrich</creatorcontrib><creatorcontrib>Hayer-Hartl, Manajit</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bracher, Andreas</au><au>Hauser, Thomas</au><au>Liu, Cuimin</au><au>Hartl, F Ulrich</au><au>Hayer-Hartl, Manajit</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural Analysis of the Rubisco-Assembly Chaperone RbcX-II from Chlamydomonas reinhardtii</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2015-08-25</date><risdate>2015</risdate><volume>10</volume><issue>8</issue><spage>e0135448</spage><epage>e0135448</epage><pages>e0135448-e0135448</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>The most prevalent form of the Rubisco enzyme is a complex of eight catalytic large subunits (RbcL) and eight regulatory small subunits (RbcS). Rubisco biogenesis depends on the assistance by specific molecular chaperones. The assembly chaperone RbcX stabilizes the RbcL subunits after folding by chaperonin and mediates their assembly to the RbcL8 core complex, from which RbcX is displaced by RbcS to form active holoenzyme. Two isoforms of RbcX are found in eukaryotes, RbcX-I, which is more closely related to cyanobacterial RbcX, and the more distant RbcX-II. The green algae Chlamydomonas reinhardtii contains only RbcX-II isoforms, CrRbcX-IIa and CrRbcX-IIb. Here we solved the crystal structure of CrRbcX-IIa and show that it forms an arc-shaped dimer with a central hydrophobic cleft for binding the C-terminal sequence of RbcL. Like other RbcX proteins, CrRbcX-IIa supports the assembly of cyanobacterial Rubisco in vitro, albeit with reduced activity relative to cyanobacterial RbcX-I. Structural analysis of a fusion protein of CrRbcX-IIa and the C-terminal peptide of RbcL suggests that the peptide binding mode of RbcX-II may differ from that of cyanobacterial RbcX. RbcX homologs appear to have adapted to their cognate Rubisco clients as a result of co-evolution.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>26305355</pmid><doi>10.1371/journal.pone.0135448</doi><oa>free_for_read</oa></addata></record> |
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| subjects | Algae Amino Acid Sequence Assembly Bacterial Proteins - chemistry Binding Binding Sites Biochemistry Biosynthesis Catalysis Chaperones Chlamydomonas reinhardtii Chlamydomonas reinhardtii - chemistry Chlorophyta Chloroplasts Crystal structure Crystallography Crystallography, X-Ray Cyanobacteria E coli Escherichia coli Eukaryotes Fusion protein Homology Hydrophobicity Isoforms Molecular chains Molecular Chaperones - chemistry Molecular structure Multiprotein Complexes - chemistry Peptides Plasmids Protein Binding Protein Conformation Protein Folding Proteins Ribulose-bisphosphate carboxylase Ribulose-Bisphosphate Carboxylase - chemistry Structural analysis Synechococcus Synechococcus elongatus |
| title | Structural Analysis of the Rubisco-Assembly Chaperone RbcX-II from Chlamydomonas reinhardtii |
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