Structures of D14 and D14L in the strigolactone and karrikin signaling pathways
Strigolactones (SLs) are plant hormones that inhibit shoot branching. DWARF14 (D14) inhibits rice tillering and is an SL receptor candidate in the branching inhibition pathway, whereas the close homologue DWARF14‐LIKE (D14L) participates in the signaling pathway of karrikins (KARs), which are derive...
Gespeichert in:
Veröffentlicht in: | Genes to cells : devoted to molecular & cellular mechanisms 2013-02, Vol.18 (2), p.147-160 |
---|---|
Hauptverfasser: | , , , , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 160 |
---|---|
container_issue | 2 |
container_start_page | 147 |
container_title | Genes to cells : devoted to molecular & cellular mechanisms |
container_volume | 18 |
creator | Kagiyama, Megumi Hirano, Yoshinori Mori, Tomoyuki Kim, Sun‐Yong Kyozuka, Junko Seto, Yoshiya Yamaguchi, Shinjiro Hakoshima, Toshio |
description | Strigolactones (SLs) are plant hormones that inhibit shoot branching. DWARF14 (D14) inhibits rice tillering and is an SL receptor candidate in the branching inhibition pathway, whereas the close homologue DWARF14‐LIKE (D14L) participates in the signaling pathway of karrikins (KARs), which are derived from burnt vegetation as smoke stimulants of seed germination. We provide the first evidence for direct binding of the bioactive SL analogue GR24 to D14. Isothermal titration calorimetry measurements show a D14–GR24 binding affinity in the sub‐micromolar range. Similarly, bioactive KAR1 directly binds D14L in the micromolar range. The crystal structure of rice D14 shows a compact α‐/β‐fold hydrolase domain forming a deep ligand‐binding pocket capable of accommodating GR24. Insertion of four α‐helices between β6 strand and αD helix forms the helical cap of the pocket, although the pocket is open to the solvent. The pocket contains the conserved catalytic triad Ser‐His‐Asp aligned with the oxyanion hole, suggesting hydrolase activity. Although these structural characteristics are conserved in D14L, the D14L pocket is smaller than that of D14. The KAR‐insensitive mutation kai2‐1 is located at the prominent long β6‐αD1 loop, which is characteristic in D14 and D14L, but not in related α‐/β‐fold hydrolases. |
doi_str_mv | 10.1111/gtc.12025 |
format | Article |
fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_1315620079</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2873930801</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4185-9a39282d9033941a72874bfcb2ba5ac66065f1bf4c759efaedc3bd1a5e64d4ef3</originalsourceid><addsrcrecordid>eNqFkT9PwzAQxS0EolAY-AIoEgtLWv9PPKICBalSB8psOY6Tpk2TYjuq-u1x2sLAwi3vpPfT6e4eAHcIjlCocen1CGGI2Rm4QoSzGFNKzvue8VgwkQzAtXMrCBHBkF2CASYEIs7FFZh_eNtp31njoraInhGNVJP3OouqJvJLEzlvq7KtlfZtYw7uWllbrYPtqrJRddWU0Vb55U7t3Q24KFTtzO1Jh-Dz9WUxeYtn8-n75GkWa4pSFgtFBE5xLiAhgiKV4DShWaEznCmmNOeQswJlBdUJE6ZQJtcky5FihtOcmoIMweNx7ta2X51xXm4qp01dq8a0nZOIIMYxhIn4Hw2LQJomnAX04Q-6ajsbTuypBJMEUpIG6v5EddnG5HJrq42ye_nz1QCMj8Cuqs3-10dQ9nHJEJc8xCWni8mhId-GUoTU</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1272370438</pqid></control><display><type>article</type><title>Structures of D14 and D14L in the strigolactone and karrikin signaling pathways</title><source>MEDLINE</source><source>Access via Wiley Online Library</source><source>Freely Accessible Japanese Titles</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Wiley Online Library (Open Access Collection)</source><creator>Kagiyama, Megumi ; Hirano, Yoshinori ; Mori, Tomoyuki ; Kim, Sun‐Yong ; Kyozuka, Junko ; Seto, Yoshiya ; Yamaguchi, Shinjiro ; Hakoshima, Toshio</creator><creatorcontrib>Kagiyama, Megumi ; Hirano, Yoshinori ; Mori, Tomoyuki ; Kim, Sun‐Yong ; Kyozuka, Junko ; Seto, Yoshiya ; Yamaguchi, Shinjiro ; Hakoshima, Toshio</creatorcontrib><description>Strigolactones (SLs) are plant hormones that inhibit shoot branching. DWARF14 (D14) inhibits rice tillering and is an SL receptor candidate in the branching inhibition pathway, whereas the close homologue DWARF14‐LIKE (D14L) participates in the signaling pathway of karrikins (KARs), which are derived from burnt vegetation as smoke stimulants of seed germination. We provide the first evidence for direct binding of the bioactive SL analogue GR24 to D14. Isothermal titration calorimetry measurements show a D14–GR24 binding affinity in the sub‐micromolar range. Similarly, bioactive KAR1 directly binds D14L in the micromolar range. The crystal structure of rice D14 shows a compact α‐/β‐fold hydrolase domain forming a deep ligand‐binding pocket capable of accommodating GR24. Insertion of four α‐helices between β6 strand and αD helix forms the helical cap of the pocket, although the pocket is open to the solvent. The pocket contains the conserved catalytic triad Ser‐His‐Asp aligned with the oxyanion hole, suggesting hydrolase activity. Although these structural characteristics are conserved in D14L, the D14L pocket is smaller than that of D14. The KAR‐insensitive mutation kai2‐1 is located at the prominent long β6‐αD1 loop, which is characteristic in D14 and D14L, but not in related α‐/β‐fold hydrolases.</description><identifier>ISSN: 1356-9597</identifier><identifier>EISSN: 1365-2443</identifier><identifier>DOI: 10.1111/gtc.12025</identifier><identifier>PMID: 23301669</identifier><identifier>CODEN: GECEFL</identifier><language>eng</language><publisher>England: Wiley Subscription Services, Inc</publisher><subject>Amino Acid Sequence ; Catalytic Domain ; Crystal structure ; Enzymes ; Furans - metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Oryza - genetics ; Oryza - metabolism ; Oryza sativa ; Plant Growth Regulators - chemistry ; Plant Growth Regulators - metabolism ; Plant Proteins - chemistry ; Plant Proteins - metabolism ; Protein Binding ; Protein Conformation ; Protein Stability ; Pyrans - metabolism ; Sequence Alignment ; Signal Transduction</subject><ispartof>Genes to cells : devoted to molecular & cellular mechanisms, 2013-02, Vol.18 (2), p.147-160</ispartof><rights>2013 The Authors Genes to Cells © 2013 by the Molecular Biology Society of Japan and Wiley Publishing Asia Pty Ltd</rights><rights>2013 The Authors Genes to Cells © 2013 by the Molecular Biology Society of Japan and Wiley Publishing Asia Pty Ltd.</rights><rights>2013 by the Molecular Biology Society of Japan/Wiley Publishing Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4185-9a39282d9033941a72874bfcb2ba5ac66065f1bf4c759efaedc3bd1a5e64d4ef3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fgtc.12025$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fgtc.12025$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>315,781,785,1418,1434,27929,27930,45579,45580,46414,46838</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23301669$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kagiyama, Megumi</creatorcontrib><creatorcontrib>Hirano, Yoshinori</creatorcontrib><creatorcontrib>Mori, Tomoyuki</creatorcontrib><creatorcontrib>Kim, Sun‐Yong</creatorcontrib><creatorcontrib>Kyozuka, Junko</creatorcontrib><creatorcontrib>Seto, Yoshiya</creatorcontrib><creatorcontrib>Yamaguchi, Shinjiro</creatorcontrib><creatorcontrib>Hakoshima, Toshio</creatorcontrib><title>Structures of D14 and D14L in the strigolactone and karrikin signaling pathways</title><title>Genes to cells : devoted to molecular & cellular mechanisms</title><addtitle>Genes Cells</addtitle><description>Strigolactones (SLs) are plant hormones that inhibit shoot branching. DWARF14 (D14) inhibits rice tillering and is an SL receptor candidate in the branching inhibition pathway, whereas the close homologue DWARF14‐LIKE (D14L) participates in the signaling pathway of karrikins (KARs), which are derived from burnt vegetation as smoke stimulants of seed germination. We provide the first evidence for direct binding of the bioactive SL analogue GR24 to D14. Isothermal titration calorimetry measurements show a D14–GR24 binding affinity in the sub‐micromolar range. Similarly, bioactive KAR1 directly binds D14L in the micromolar range. The crystal structure of rice D14 shows a compact α‐/β‐fold hydrolase domain forming a deep ligand‐binding pocket capable of accommodating GR24. Insertion of four α‐helices between β6 strand and αD helix forms the helical cap of the pocket, although the pocket is open to the solvent. The pocket contains the conserved catalytic triad Ser‐His‐Asp aligned with the oxyanion hole, suggesting hydrolase activity. Although these structural characteristics are conserved in D14L, the D14L pocket is smaller than that of D14. The KAR‐insensitive mutation kai2‐1 is located at the prominent long β6‐αD1 loop, which is characteristic in D14 and D14L, but not in related α‐/β‐fold hydrolases.</description><subject>Amino Acid Sequence</subject><subject>Catalytic Domain</subject><subject>Crystal structure</subject><subject>Enzymes</subject><subject>Furans - metabolism</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Oryza - genetics</subject><subject>Oryza - metabolism</subject><subject>Oryza sativa</subject><subject>Plant Growth Regulators - chemistry</subject><subject>Plant Growth Regulators - metabolism</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - metabolism</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Protein Stability</subject><subject>Pyrans - metabolism</subject><subject>Sequence Alignment</subject><subject>Signal Transduction</subject><issn>1356-9597</issn><issn>1365-2443</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkT9PwzAQxS0EolAY-AIoEgtLWv9PPKICBalSB8psOY6Tpk2TYjuq-u1x2sLAwi3vpPfT6e4eAHcIjlCocen1CGGI2Rm4QoSzGFNKzvue8VgwkQzAtXMrCBHBkF2CASYEIs7FFZh_eNtp31njoraInhGNVJP3OouqJvJLEzlvq7KtlfZtYw7uWllbrYPtqrJRddWU0Vb55U7t3Q24KFTtzO1Jh-Dz9WUxeYtn8-n75GkWa4pSFgtFBE5xLiAhgiKV4DShWaEznCmmNOeQswJlBdUJE6ZQJtcky5FihtOcmoIMweNx7ta2X51xXm4qp01dq8a0nZOIIMYxhIn4Hw2LQJomnAX04Q-6ajsbTuypBJMEUpIG6v5EddnG5HJrq42ye_nz1QCMj8Cuqs3-10dQ9nHJEJc8xCWni8mhId-GUoTU</recordid><startdate>201302</startdate><enddate>201302</enddate><creator>Kagiyama, Megumi</creator><creator>Hirano, Yoshinori</creator><creator>Mori, Tomoyuki</creator><creator>Kim, Sun‐Yong</creator><creator>Kyozuka, Junko</creator><creator>Seto, Yoshiya</creator><creator>Yamaguchi, Shinjiro</creator><creator>Hakoshima, Toshio</creator><general>Wiley Subscription Services, Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7TK</scope><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>201302</creationdate><title>Structures of D14 and D14L in the strigolactone and karrikin signaling pathways</title><author>Kagiyama, Megumi ; Hirano, Yoshinori ; Mori, Tomoyuki ; Kim, Sun‐Yong ; Kyozuka, Junko ; Seto, Yoshiya ; Yamaguchi, Shinjiro ; Hakoshima, Toshio</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4185-9a39282d9033941a72874bfcb2ba5ac66065f1bf4c759efaedc3bd1a5e64d4ef3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Amino Acid Sequence</topic><topic>Catalytic Domain</topic><topic>Crystal structure</topic><topic>Enzymes</topic><topic>Furans - metabolism</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Oryza - genetics</topic><topic>Oryza - metabolism</topic><topic>Oryza sativa</topic><topic>Plant Growth Regulators - chemistry</topic><topic>Plant Growth Regulators - metabolism</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - metabolism</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Protein Stability</topic><topic>Pyrans - metabolism</topic><topic>Sequence Alignment</topic><topic>Signal Transduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kagiyama, Megumi</creatorcontrib><creatorcontrib>Hirano, Yoshinori</creatorcontrib><creatorcontrib>Mori, Tomoyuki</creatorcontrib><creatorcontrib>Kim, Sun‐Yong</creatorcontrib><creatorcontrib>Kyozuka, Junko</creatorcontrib><creatorcontrib>Seto, Yoshiya</creatorcontrib><creatorcontrib>Yamaguchi, Shinjiro</creatorcontrib><creatorcontrib>Hakoshima, Toshio</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Genes to cells : devoted to molecular & cellular mechanisms</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kagiyama, Megumi</au><au>Hirano, Yoshinori</au><au>Mori, Tomoyuki</au><au>Kim, Sun‐Yong</au><au>Kyozuka, Junko</au><au>Seto, Yoshiya</au><au>Yamaguchi, Shinjiro</au><au>Hakoshima, Toshio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structures of D14 and D14L in the strigolactone and karrikin signaling pathways</atitle><jtitle>Genes to cells : devoted to molecular & cellular mechanisms</jtitle><addtitle>Genes Cells</addtitle><date>2013-02</date><risdate>2013</risdate><volume>18</volume><issue>2</issue><spage>147</spage><epage>160</epage><pages>147-160</pages><issn>1356-9597</issn><eissn>1365-2443</eissn><coden>GECEFL</coden><abstract>Strigolactones (SLs) are plant hormones that inhibit shoot branching. DWARF14 (D14) inhibits rice tillering and is an SL receptor candidate in the branching inhibition pathway, whereas the close homologue DWARF14‐LIKE (D14L) participates in the signaling pathway of karrikins (KARs), which are derived from burnt vegetation as smoke stimulants of seed germination. We provide the first evidence for direct binding of the bioactive SL analogue GR24 to D14. Isothermal titration calorimetry measurements show a D14–GR24 binding affinity in the sub‐micromolar range. Similarly, bioactive KAR1 directly binds D14L in the micromolar range. The crystal structure of rice D14 shows a compact α‐/β‐fold hydrolase domain forming a deep ligand‐binding pocket capable of accommodating GR24. Insertion of four α‐helices between β6 strand and αD helix forms the helical cap of the pocket, although the pocket is open to the solvent. The pocket contains the conserved catalytic triad Ser‐His‐Asp aligned with the oxyanion hole, suggesting hydrolase activity. Although these structural characteristics are conserved in D14L, the D14L pocket is smaller than that of D14. The KAR‐insensitive mutation kai2‐1 is located at the prominent long β6‐αD1 loop, which is characteristic in D14 and D14L, but not in related α‐/β‐fold hydrolases.</abstract><cop>England</cop><pub>Wiley Subscription Services, Inc</pub><pmid>23301669</pmid><doi>10.1111/gtc.12025</doi><tpages>14</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1356-9597 |
ispartof | Genes to cells : devoted to molecular & cellular mechanisms, 2013-02, Vol.18 (2), p.147-160 |
issn | 1356-9597 1365-2443 |
language | eng |
recordid | cdi_proquest_miscellaneous_1315620079 |
source | MEDLINE; Access via Wiley Online Library; Freely Accessible Japanese Titles; EZB-FREE-00999 freely available EZB journals; Wiley Online Library (Open Access Collection) |
subjects | Amino Acid Sequence Catalytic Domain Crystal structure Enzymes Furans - metabolism Models, Molecular Molecular Sequence Data Mutation Oryza - genetics Oryza - metabolism Oryza sativa Plant Growth Regulators - chemistry Plant Growth Regulators - metabolism Plant Proteins - chemistry Plant Proteins - metabolism Protein Binding Protein Conformation Protein Stability Pyrans - metabolism Sequence Alignment Signal Transduction |
title | Structures of D14 and D14L in the strigolactone and karrikin signaling pathways |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-10T22%3A11%3A52IST&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=Structures%20of%20D14%20and%20D14L%20in%20the%20strigolactone%20and%20karrikin%20signaling%20pathways&rft.jtitle=Genes%20to%20cells%20:%20devoted%20to%20molecular%20&%20cellular%20mechanisms&rft.au=Kagiyama,%20Megumi&rft.date=2013-02&rft.volume=18&rft.issue=2&rft.spage=147&rft.epage=160&rft.pages=147-160&rft.issn=1356-9597&rft.eissn=1365-2443&rft.coden=GECEFL&rft_id=info:doi/10.1111/gtc.12025&rft_dat=%3Cproquest_pubme%3E2873930801%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=1272370438&rft_id=info:pmid/23301669&rfr_iscdi=true |