A Dynamic cpSRP43-Albino3 Interaction Mediates Translocase Regulation of Chloroplast Signal Recognition Particle (cpSRP)-targeting Components
The chloroplast signal recognition particle (cpSRP) and its receptor, chloroplast FtsY (cpFtsY), form an essential complex with the translocase Albino3 (Alb3) during post-translational targeting of light-harvesting chlorophyll-binding proteins (LHCPs). Here, we describe a combination of studies that...
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| Veröffentlicht in: | The Journal of biological chemistry 2010-10, Vol.285 (44), p.34220-34230 |
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| container_title | The Journal of biological chemistry |
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| creator | Lewis, Nathaniel E. Marty, Naomi J. Kathir, Karuppanan Muthusamy Rajalingam, Dakshinamurthy Kight, Alicia D. Daily, Anna Kumar, Thallapuranam Krishnaswamy Suresh Henry, Ralph L. Goforth, Robyn L. |
| description | The chloroplast signal recognition particle (cpSRP) and its receptor, chloroplast FtsY (cpFtsY), form an essential complex with the translocase Albino3 (Alb3) during post-translational targeting of light-harvesting chlorophyll-binding proteins (LHCPs). Here, we describe a combination of studies that explore the binding interface and functional role of a previously identified cpSRP43-Alb3 interaction. Using recombinant proteins corresponding to the C terminus of Alb3 (Alb3-Cterm) and various domains of cpSRP43, we identify the ankyrin repeat region of cpSRP43 as the domain primarily responsible for the interaction with Alb3-Cterm. Furthermore, we show Alb3-Cterm dissociates a cpSRP·LHCP targeting complex in vitro and stimulates GTP hydrolysis by cpSRP54 and cpFtsY in a strictly cpSRP43-dependent manner. These results support a model in which interactions between the ankyrin region of cpSRP43 and the C terminus of Alb3 promote distinct membrane-localized events, including LHCP release from cpSRP and release of targeting components from Alb3. |
| doi_str_mv | 10.1074/jbc.M110.160093 |
| format | Article |
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Here, we describe a combination of studies that explore the binding interface and functional role of a previously identified cpSRP43-Alb3 interaction. Using recombinant proteins corresponding to the C terminus of Alb3 (Alb3-Cterm) and various domains of cpSRP43, we identify the ankyrin repeat region of cpSRP43 as the domain primarily responsible for the interaction with Alb3-Cterm. Furthermore, we show Alb3-Cterm dissociates a cpSRP·LHCP targeting complex in vitro and stimulates GTP hydrolysis by cpSRP54 and cpFtsY in a strictly cpSRP43-dependent manner. These results support a model in which interactions between the ankyrin region of cpSRP43 and the C terminus of Alb3 promote distinct membrane-localized events, including LHCP release from cpSRP and release of targeting components from Alb3.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M110.160093</identifier><identifier>PMID: 20729200</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Albino3 ; Arabidopsis Proteins - metabolism ; Cell Membrane - metabolism ; Chloroplast ; Chloroplast Proteins ; Chloroplasts - metabolism ; Cloning, Molecular ; GTP Regulation ; Guanosine Triphosphate - chemistry ; Hydrolysis ; Membrane Biology ; Membrane Proteins ; Membrane Targeting ; Models, Biological ; Pisum sativum - metabolism ; Plant Biology ; Protein Binding ; Protein Interaction Mapping ; Protein Structure, Tertiary ; Protein Targeting ; Protein Translocation ; Protein Transport ; Protein-Protein Interactions ; Recombinant Proteins - chemistry ; Signal Recognition Particle ; Signal Recognition Particle - metabolism ; Thylakoids - metabolism</subject><ispartof>The Journal of biological chemistry, 2010-10, Vol.285 (44), p.34220-34230</ispartof><rights>2010 © 2010 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>2010 by The American Society for Biochemistry and Molecular Biology, Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c508t-9ac0489c15a07dfd6ca00d5dee544092d2b816692d4be47b59ff28d9cbbbf9de3</citedby><cites>FETCH-LOGICAL-c508t-9ac0489c15a07dfd6ca00d5dee544092d2b816692d4be47b59ff28d9cbbbf9de3</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/PMC2962520/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2962520/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20729200$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lewis, Nathaniel E.</creatorcontrib><creatorcontrib>Marty, Naomi J.</creatorcontrib><creatorcontrib>Kathir, Karuppanan Muthusamy</creatorcontrib><creatorcontrib>Rajalingam, Dakshinamurthy</creatorcontrib><creatorcontrib>Kight, Alicia D.</creatorcontrib><creatorcontrib>Daily, Anna</creatorcontrib><creatorcontrib>Kumar, Thallapuranam Krishnaswamy Suresh</creatorcontrib><creatorcontrib>Henry, Ralph L.</creatorcontrib><creatorcontrib>Goforth, Robyn L.</creatorcontrib><title>A Dynamic cpSRP43-Albino3 Interaction Mediates Translocase Regulation of Chloroplast Signal Recognition Particle (cpSRP)-targeting Components</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The chloroplast signal recognition particle (cpSRP) and its receptor, chloroplast FtsY (cpFtsY), form an essential complex with the translocase Albino3 (Alb3) during post-translational targeting of light-harvesting chlorophyll-binding proteins (LHCPs). Here, we describe a combination of studies that explore the binding interface and functional role of a previously identified cpSRP43-Alb3 interaction. Using recombinant proteins corresponding to the C terminus of Alb3 (Alb3-Cterm) and various domains of cpSRP43, we identify the ankyrin repeat region of cpSRP43 as the domain primarily responsible for the interaction with Alb3-Cterm. Furthermore, we show Alb3-Cterm dissociates a cpSRP·LHCP targeting complex in vitro and stimulates GTP hydrolysis by cpSRP54 and cpFtsY in a strictly cpSRP43-dependent manner. These results support a model in which interactions between the ankyrin region of cpSRP43 and the C terminus of Alb3 promote distinct membrane-localized events, including LHCP release from cpSRP and release of targeting components from Alb3.</description><subject>Albino3</subject><subject>Arabidopsis Proteins - metabolism</subject><subject>Cell Membrane - metabolism</subject><subject>Chloroplast</subject><subject>Chloroplast Proteins</subject><subject>Chloroplasts - metabolism</subject><subject>Cloning, Molecular</subject><subject>GTP Regulation</subject><subject>Guanosine Triphosphate - chemistry</subject><subject>Hydrolysis</subject><subject>Membrane Biology</subject><subject>Membrane Proteins</subject><subject>Membrane Targeting</subject><subject>Models, Biological</subject><subject>Pisum sativum - metabolism</subject><subject>Plant Biology</subject><subject>Protein Binding</subject><subject>Protein Interaction Mapping</subject><subject>Protein Structure, Tertiary</subject><subject>Protein Targeting</subject><subject>Protein Translocation</subject><subject>Protein Transport</subject><subject>Protein-Protein Interactions</subject><subject>Recombinant Proteins - chemistry</subject><subject>Signal Recognition Particle</subject><subject>Signal Recognition Particle - metabolism</subject><subject>Thylakoids - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kU1vVCEUhonR2Gl17c6w0y5uC1zuBxuTyfjVpI1NWxN3hAvn3tIwcAWmSX-E_1lmpja6kA2cnIf3EB6E3lByQknHT-8GfXJBt1VLiKifoQUlfV3VDf3xHC0IYbQSrOkP0GFKd6QsLuhLdMBIxwQjZIF-LfHHB6_WVmM9X19d8rpausH6UOMznyEqnW3w-AKMVRkSvonKJxe0SoCvYNo4teuHEa9uXYhhdiplfG0nr1wBdJi83RGXKmarHeD3uznHVVZxgmz9hFdhPQcPPqdX6MWoXILXj_sR-v75083qa3X-7cvZanle6Yb0uRJKE94LTRtFOjOaVitCTGMAGs6JYIYNPW3bcuAD8G5oxDiy3gg9DMMoDNRH6MM-d94MazC6zI7KyTnatYoPMigr_-14eyuncC-ZaFnDSAl49xgQw88NpCzXNmlwTnkImyS7lrCac9YV8nRP6hhSijA-TaFEbh3K4lBuHcq9w3Lj7d-Pe-L_SCuA2ANQvujeQpRJW_C6OIqgszTB_jf8N-Q6rtY</recordid><startdate>20101029</startdate><enddate>20101029</enddate><creator>Lewis, Nathaniel E.</creator><creator>Marty, Naomi J.</creator><creator>Kathir, Karuppanan Muthusamy</creator><creator>Rajalingam, Dakshinamurthy</creator><creator>Kight, Alicia D.</creator><creator>Daily, Anna</creator><creator>Kumar, Thallapuranam Krishnaswamy Suresh</creator><creator>Henry, Ralph L.</creator><creator>Goforth, Robyn L.</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>20101029</creationdate><title>A Dynamic cpSRP43-Albino3 Interaction Mediates Translocase Regulation of Chloroplast Signal Recognition Particle (cpSRP)-targeting Components</title><author>Lewis, Nathaniel E. ; Marty, Naomi J. ; Kathir, Karuppanan Muthusamy ; Rajalingam, Dakshinamurthy ; Kight, Alicia D. ; Daily, Anna ; Kumar, Thallapuranam Krishnaswamy Suresh ; Henry, Ralph L. ; Goforth, Robyn L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c508t-9ac0489c15a07dfd6ca00d5dee544092d2b816692d4be47b59ff28d9cbbbf9de3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Albino3</topic><topic>Arabidopsis Proteins - metabolism</topic><topic>Cell Membrane - metabolism</topic><topic>Chloroplast</topic><topic>Chloroplast Proteins</topic><topic>Chloroplasts - metabolism</topic><topic>Cloning, Molecular</topic><topic>GTP Regulation</topic><topic>Guanosine Triphosphate - chemistry</topic><topic>Hydrolysis</topic><topic>Membrane Biology</topic><topic>Membrane Proteins</topic><topic>Membrane Targeting</topic><topic>Models, Biological</topic><topic>Pisum sativum - metabolism</topic><topic>Plant Biology</topic><topic>Protein Binding</topic><topic>Protein Interaction Mapping</topic><topic>Protein Structure, Tertiary</topic><topic>Protein Targeting</topic><topic>Protein Translocation</topic><topic>Protein Transport</topic><topic>Protein-Protein Interactions</topic><topic>Recombinant Proteins - chemistry</topic><topic>Signal Recognition Particle</topic><topic>Signal Recognition Particle - metabolism</topic><topic>Thylakoids - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lewis, Nathaniel E.</creatorcontrib><creatorcontrib>Marty, Naomi J.</creatorcontrib><creatorcontrib>Kathir, Karuppanan Muthusamy</creatorcontrib><creatorcontrib>Rajalingam, Dakshinamurthy</creatorcontrib><creatorcontrib>Kight, Alicia D.</creatorcontrib><creatorcontrib>Daily, Anna</creatorcontrib><creatorcontrib>Kumar, Thallapuranam Krishnaswamy Suresh</creatorcontrib><creatorcontrib>Henry, Ralph L.</creatorcontrib><creatorcontrib>Goforth, Robyn L.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lewis, Nathaniel E.</au><au>Marty, Naomi J.</au><au>Kathir, Karuppanan Muthusamy</au><au>Rajalingam, Dakshinamurthy</au><au>Kight, Alicia D.</au><au>Daily, Anna</au><au>Kumar, Thallapuranam Krishnaswamy Suresh</au><au>Henry, Ralph L.</au><au>Goforth, Robyn L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Dynamic cpSRP43-Albino3 Interaction Mediates Translocase Regulation of Chloroplast Signal Recognition Particle (cpSRP)-targeting Components</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2010-10-29</date><risdate>2010</risdate><volume>285</volume><issue>44</issue><spage>34220</spage><epage>34230</epage><pages>34220-34230</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The chloroplast signal recognition particle (cpSRP) and its receptor, chloroplast FtsY (cpFtsY), form an essential complex with the translocase Albino3 (Alb3) during post-translational targeting of light-harvesting chlorophyll-binding proteins (LHCPs). Here, we describe a combination of studies that explore the binding interface and functional role of a previously identified cpSRP43-Alb3 interaction. Using recombinant proteins corresponding to the C terminus of Alb3 (Alb3-Cterm) and various domains of cpSRP43, we identify the ankyrin repeat region of cpSRP43 as the domain primarily responsible for the interaction with Alb3-Cterm. Furthermore, we show Alb3-Cterm dissociates a cpSRP·LHCP targeting complex in vitro and stimulates GTP hydrolysis by cpSRP54 and cpFtsY in a strictly cpSRP43-dependent manner. These results support a model in which interactions between the ankyrin region of cpSRP43 and the C terminus of Alb3 promote distinct membrane-localized events, including LHCP release from cpSRP and release of targeting components from Alb3.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>20729200</pmid><doi>10.1074/jbc.M110.160093</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Albino3 Arabidopsis Proteins - metabolism Cell Membrane - metabolism Chloroplast Chloroplast Proteins Chloroplasts - metabolism Cloning, Molecular GTP Regulation Guanosine Triphosphate - chemistry Hydrolysis Membrane Biology Membrane Proteins Membrane Targeting Models, Biological Pisum sativum - metabolism Plant Biology Protein Binding Protein Interaction Mapping Protein Structure, Tertiary Protein Targeting Protein Translocation Protein Transport Protein-Protein Interactions Recombinant Proteins - chemistry Signal Recognition Particle Signal Recognition Particle - metabolism Thylakoids - metabolism |
| title | A Dynamic cpSRP43-Albino3 Interaction Mediates Translocase Regulation of Chloroplast Signal Recognition Particle (cpSRP)-targeting Components |
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