Regulation of the GTPase Cycle in Post-translational Signal Recognition Particle-based Protein Targeting Involves cpSRP43
The chloroplast signal recognition particle consists of a conserved 54-kDa GTPase and a novel 43-kDa chromodomain protein (cpSRP43) that together bind light-harvesting chlorophyll a/b-binding protein (LHCP) to form a soluble targeting complex that is subsequently directed to the thylakoid membrane....
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| Veröffentlicht in: | The Journal of biological chemistry 2004-10, Vol.279 (41), p.43077-43084 |
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| container_issue | 41 |
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| container_title | The Journal of biological chemistry |
| container_volume | 279 |
| creator | Goforth, Robyn L Peterson, Eric C Yuan, Jianguo Moore, Misty J Kight, Alicia D Lohse, Matthew B Sakon, Joshua Henry, Ralph L |
| description | The chloroplast signal recognition particle consists of a conserved 54-kDa GTPase and a novel 43-kDa chromodomain protein
(cpSRP43) that together bind light-harvesting chlorophyll a/b-binding protein (LHCP) to form a soluble targeting complex that
is subsequently directed to the thylakoid membrane. Homology-based modeling of cpSRP43 indicates the presence of two previously
identified chromodomains along with a third N-terminal chromodomain. Chromodomain deletion constructs were used to examine
the role of each chromodomain in mediating distinct steps in the LHCP localization mechanism. The C-terminal chromodomain
is completely dispensable for LHCP targeting/integration in vitro . The central chromodomain is essential for both targeting complex formation and integration because of its role in binding
the M domain of cpSRP54. The N-terminal chromodomain (CD1) is unnecessary for targeting complex formation but is required
for integration. This correlates with the ability of CD1 along with the ankyrin repeat region of cpSRP43 to regulate the GTPase
cycle of the cpSRP-receptor complex. |
| doi_str_mv | 10.1074/jbc.M401600200 |
| format | Article |
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(cpSRP43) that together bind light-harvesting chlorophyll a/b-binding protein (LHCP) to form a soluble targeting complex that
is subsequently directed to the thylakoid membrane. Homology-based modeling of cpSRP43 indicates the presence of two previously
identified chromodomains along with a third N-terminal chromodomain. Chromodomain deletion constructs were used to examine
the role of each chromodomain in mediating distinct steps in the LHCP localization mechanism. The C-terminal chromodomain
is completely dispensable for LHCP targeting/integration in vitro . The central chromodomain is essential for both targeting complex formation and integration because of its role in binding
the M domain of cpSRP54. The N-terminal chromodomain (CD1) is unnecessary for targeting complex formation but is required
for integration. This correlates with the ability of CD1 along with the ankyrin repeat region of cpSRP43 to regulate the GTPase
cycle of the cpSRP-receptor complex.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M401600200</identifier><identifier>PMID: 15292240</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Ankyrins - chemistry ; Apoproteins - chemistry ; Arabidopsis ; Biological Transport ; Chloroplast Proteins ; Chloroplasts - chemistry ; Chloroplasts - metabolism ; Cloning, Molecular ; Electrophoresis, Polyacrylamide Gel ; Endoplasmic Reticulum - metabolism ; Gene Deletion ; Glutathione Transferase - metabolism ; GTP Phosphohydrolases - chemistry ; Hydrolysis ; Models, Molecular ; Molecular Sequence Data ; Peptides - chemistry ; Photosystem II Protein Complex - chemistry ; Plant Proteins - chemistry ; Protein Biosynthesis ; Protein Processing, Post-Translational ; Protein Structure, Tertiary ; Recombinant Fusion Proteins - chemistry ; Ribosomes - chemistry ; Signal Recognition Particle - chemistry ; Signal Recognition Particle - physiology ; Signal Transduction ; Thylakoids - metabolism ; Two-Hybrid System Techniques</subject><ispartof>The Journal of biological chemistry, 2004-10, Vol.279 (41), p.43077-43084</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c360t-6c83e75c7b21178d083513d649cdfec0a8ac0f736461635266cb9d9d080035b23</citedby><cites>FETCH-LOGICAL-c360t-6c83e75c7b21178d083513d649cdfec0a8ac0f736461635266cb9d9d080035b23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15292240$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Goforth, Robyn L</creatorcontrib><creatorcontrib>Peterson, Eric C</creatorcontrib><creatorcontrib>Yuan, Jianguo</creatorcontrib><creatorcontrib>Moore, Misty J</creatorcontrib><creatorcontrib>Kight, Alicia D</creatorcontrib><creatorcontrib>Lohse, Matthew B</creatorcontrib><creatorcontrib>Sakon, Joshua</creatorcontrib><creatorcontrib>Henry, Ralph L</creatorcontrib><title>Regulation of the GTPase Cycle in Post-translational Signal Recognition Particle-based Protein Targeting Involves cpSRP43</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The chloroplast signal recognition particle consists of a conserved 54-kDa GTPase and a novel 43-kDa chromodomain protein
(cpSRP43) that together bind light-harvesting chlorophyll a/b-binding protein (LHCP) to form a soluble targeting complex that
is subsequently directed to the thylakoid membrane. Homology-based modeling of cpSRP43 indicates the presence of two previously
identified chromodomains along with a third N-terminal chromodomain. Chromodomain deletion constructs were used to examine
the role of each chromodomain in mediating distinct steps in the LHCP localization mechanism. The C-terminal chromodomain
is completely dispensable for LHCP targeting/integration in vitro . The central chromodomain is essential for both targeting complex formation and integration because of its role in binding
the M domain of cpSRP54. The N-terminal chromodomain (CD1) is unnecessary for targeting complex formation but is required
for integration. This correlates with the ability of CD1 along with the ankyrin repeat region of cpSRP43 to regulate the GTPase
cycle of the cpSRP-receptor complex.</description><subject>Amino Acid Sequence</subject><subject>Ankyrins - chemistry</subject><subject>Apoproteins - chemistry</subject><subject>Arabidopsis</subject><subject>Biological Transport</subject><subject>Chloroplast Proteins</subject><subject>Chloroplasts - chemistry</subject><subject>Chloroplasts - metabolism</subject><subject>Cloning, Molecular</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Gene Deletion</subject><subject>Glutathione Transferase - metabolism</subject><subject>GTP Phosphohydrolases - chemistry</subject><subject>Hydrolysis</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Peptides - chemistry</subject><subject>Photosystem II Protein Complex - chemistry</subject><subject>Plant Proteins - chemistry</subject><subject>Protein Biosynthesis</subject><subject>Protein Processing, Post-Translational</subject><subject>Protein Structure, Tertiary</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Ribosomes - chemistry</subject><subject>Signal Recognition Particle - chemistry</subject><subject>Signal Recognition Particle - physiology</subject><subject>Signal Transduction</subject><subject>Thylakoids - metabolism</subject><subject>Two-Hybrid System Techniques</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkM9LwzAUx4MoOqdXj5KD186XH03bowydg4llm-AtpGnaZXTtSLrJ_nszN_BdvvD4fB68L0IPBEYEEv68LvTogwMRABTgAg0IpCxiMfm-RIOwI1FG4_QG3Xq_hjA8I9fohsQ0o5TDAB3mpt41qrddi7sK9yuDJ8tceYPHB90YbFucd76Peqdaf-JUgxe2Psbc6K5u7Z-cK9fbYERFkEucu643QV4qV5vetjWetvuu2RuP9XYxzzm7Q1eVary5P-cQfb29Lsfv0exzMh2_zCLNBPSR0CkzSayTghKSpGV4LyasFDzTZWU0qFRpqBImuCCCxVQIXWRlFjgAFheUDdHodFe7zntnKrl1dqPcQRKQxw5l6FD-dxiEx5Ow3RUbU_7j59IC8HQCVrZe_VhnZGE7vTIbSZNMciI5gyRhvxb8eSY</recordid><startdate>20041008</startdate><enddate>20041008</enddate><creator>Goforth, Robyn L</creator><creator>Peterson, Eric C</creator><creator>Yuan, Jianguo</creator><creator>Moore, Misty J</creator><creator>Kight, Alicia D</creator><creator>Lohse, Matthew B</creator><creator>Sakon, Joshua</creator><creator>Henry, Ralph L</creator><general>American Society for Biochemistry and Molecular Biology</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></search><sort><creationdate>20041008</creationdate><title>Regulation of the GTPase Cycle in Post-translational Signal Recognition Particle-based Protein Targeting Involves cpSRP43</title><author>Goforth, Robyn L ; Peterson, Eric C ; Yuan, Jianguo ; Moore, Misty J ; Kight, Alicia D ; Lohse, Matthew B ; Sakon, Joshua ; Henry, Ralph L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c360t-6c83e75c7b21178d083513d649cdfec0a8ac0f736461635266cb9d9d080035b23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Amino Acid Sequence</topic><topic>Ankyrins - chemistry</topic><topic>Apoproteins - chemistry</topic><topic>Arabidopsis</topic><topic>Biological Transport</topic><topic>Chloroplast Proteins</topic><topic>Chloroplasts - chemistry</topic><topic>Chloroplasts - metabolism</topic><topic>Cloning, Molecular</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Gene Deletion</topic><topic>Glutathione Transferase - metabolism</topic><topic>GTP Phosphohydrolases - chemistry</topic><topic>Hydrolysis</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Peptides - chemistry</topic><topic>Photosystem II Protein Complex - chemistry</topic><topic>Plant Proteins - chemistry</topic><topic>Protein Biosynthesis</topic><topic>Protein Processing, Post-Translational</topic><topic>Protein Structure, Tertiary</topic><topic>Recombinant Fusion Proteins - chemistry</topic><topic>Ribosomes - chemistry</topic><topic>Signal Recognition Particle - chemistry</topic><topic>Signal Recognition Particle - physiology</topic><topic>Signal Transduction</topic><topic>Thylakoids - metabolism</topic><topic>Two-Hybrid System Techniques</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Goforth, Robyn L</creatorcontrib><creatorcontrib>Peterson, Eric C</creatorcontrib><creatorcontrib>Yuan, Jianguo</creatorcontrib><creatorcontrib>Moore, Misty J</creatorcontrib><creatorcontrib>Kight, Alicia D</creatorcontrib><creatorcontrib>Lohse, Matthew B</creatorcontrib><creatorcontrib>Sakon, Joshua</creatorcontrib><creatorcontrib>Henry, Ralph L</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Goforth, Robyn L</au><au>Peterson, Eric C</au><au>Yuan, Jianguo</au><au>Moore, Misty J</au><au>Kight, Alicia D</au><au>Lohse, Matthew B</au><au>Sakon, Joshua</au><au>Henry, Ralph L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Regulation of the GTPase Cycle in Post-translational Signal Recognition Particle-based Protein Targeting Involves cpSRP43</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2004-10-08</date><risdate>2004</risdate><volume>279</volume><issue>41</issue><spage>43077</spage><epage>43084</epage><pages>43077-43084</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The chloroplast signal recognition particle consists of a conserved 54-kDa GTPase and a novel 43-kDa chromodomain protein
(cpSRP43) that together bind light-harvesting chlorophyll a/b-binding protein (LHCP) to form a soluble targeting complex that
is subsequently directed to the thylakoid membrane. Homology-based modeling of cpSRP43 indicates the presence of two previously
identified chromodomains along with a third N-terminal chromodomain. Chromodomain deletion constructs were used to examine
the role of each chromodomain in mediating distinct steps in the LHCP localization mechanism. The C-terminal chromodomain
is completely dispensable for LHCP targeting/integration in vitro . The central chromodomain is essential for both targeting complex formation and integration because of its role in binding
the M domain of cpSRP54. The N-terminal chromodomain (CD1) is unnecessary for targeting complex formation but is required
for integration. This correlates with the ability of CD1 along with the ankyrin repeat region of cpSRP43 to regulate the GTPase
cycle of the cpSRP-receptor complex.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>15292240</pmid><doi>10.1074/jbc.M401600200</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Ankyrins - chemistry Apoproteins - chemistry Arabidopsis Biological Transport Chloroplast Proteins Chloroplasts - chemistry Chloroplasts - metabolism Cloning, Molecular Electrophoresis, Polyacrylamide Gel Endoplasmic Reticulum - metabolism Gene Deletion Glutathione Transferase - metabolism GTP Phosphohydrolases - chemistry Hydrolysis Models, Molecular Molecular Sequence Data Peptides - chemistry Photosystem II Protein Complex - chemistry Plant Proteins - chemistry Protein Biosynthesis Protein Processing, Post-Translational Protein Structure, Tertiary Recombinant Fusion Proteins - chemistry Ribosomes - chemistry Signal Recognition Particle - chemistry Signal Recognition Particle - physiology Signal Transduction Thylakoids - metabolism Two-Hybrid System Techniques |
| title | Regulation of the GTPase Cycle in Post-translational Signal Recognition Particle-based Protein Targeting Involves cpSRP43 |
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