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Structures of human SRP72 complexes provide insights into SRP RNA remodeling and ribosome interaction
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| Veröffentlicht in: | Nucleic acids research 45(2017), 1, Seite 470-481 |
|---|---|
| Personen und Körperschaften: | , , , , |
| Titel: | Structures of human SRP72 complexes provide insights into SRP RNA remodeling and ribosome interaction/ Matthias M.M. Becker, Karine Lapouge, Bernd Segnitz, Klemens Wild and Irmgard Sinning |
| Format: | E-Book-Kapitel |
| Sprache: | Englisch |
| veröffentlicht: |
2017
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| Gesamtaufnahme: |
: Nucleic acids research, 45(2017), 1, Seite 470-481
, volume:45 |
| Quelle: | Verbunddaten SWB Lizenzfreie Online-Ressourcen |
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| 245 | 1 | 0 | |a Structures of human SRP72 complexes provide insights into SRP RNA remodeling and ribosome interaction |c Matthias M.M. Becker, Karine Lapouge, Bernd Segnitz, Klemens Wild and Irmgard Sinning |
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| 520 | |a Co-translational protein targeting and membrane protein insertion is a fundamental process and depends on the signal recognition particle (SRP). In mammals, SRP is composed of the SRP RNA crucial for SRP assembly and function and six proteins. The two largest proteins SRP68 and SRP72 form a heterodimer and bind to a regulatory site of the SRP RNA. Despite their essential roles in the SRP pathway, structural information has been available only for the SRP68 RNA-binding domain (RBD). Here we present the crystal structures of the SRP68 protein-binding domain (PBD) in complex with SRP72-PBD and of the SRP72-RBD bound to the SRP S domain (SRP RNA, SRP19 and SRP68) detailing all interactions of SRP72 within SRP. The SRP72-PBD is a tetratricopeptide repeat, which binds an extended linear motif of SRP68 with high affinity. The SRP72-RBD is a flexible peptide crawling along the 5e- and 5f-loops of SRP RNA. A conserved tryptophan inserts into the 5e-loop forming a novel type of RNA kink-turn stabilized by a potassium ion, which we define as K+-turn. In addition, SRP72-RBD remodels the 5f-loop involved in ribosome binding and visualizes SRP RNA plasticity. Docking of the S domain structure into cryo-electron microscopy density maps reveals multiple contact sites between SRP68/72 and the ribosome, and explains the role of SRP72 in the SRP pathway. | ||
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| contents | Co-translational protein targeting and membrane protein insertion is a fundamental process and depends on the signal recognition particle (SRP). In mammals, SRP is composed of the SRP RNA crucial for SRP assembly and function and six proteins. The two largest proteins SRP68 and SRP72 form a heterodimer and bind to a regulatory site of the SRP RNA. Despite their essential roles in the SRP pathway, structural information has been available only for the SRP68 RNA-binding domain (RBD). Here we present the crystal structures of the SRP68 protein-binding domain (PBD) in complex with SRP72-PBD and of the SRP72-RBD bound to the SRP S domain (SRP RNA, SRP19 and SRP68) detailing all interactions of SRP72 within SRP. The SRP72-PBD is a tetratricopeptide repeat, which binds an extended linear motif of SRP68 with high affinity. The SRP72-RBD is a flexible peptide crawling along the 5e- and 5f-loops of SRP RNA. A conserved tryptophan inserts into the 5e-loop forming a novel type of RNA kink-turn stabilized by a potassium ion, which we define as K+-turn. In addition, SRP72-RBD remodels the 5f-loop involved in ribosome binding and visualizes SRP RNA plasticity. Docking of the S domain structure into cryo-electron microscopy density maps reveals multiple contact sites between SRP68/72 and the ribosome, and explains the role of SRP72 in the SRP pathway. |
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| spelling | Becker, Matthias Michael Markus VerfasserIn (DE-588)1129722600 (DE-627)884368513 (DE-576)486520447 aut, Structures of human SRP72 complexes provide insights into SRP RNA remodeling and ribosome interaction Matthias M.M. Becker, Karine Lapouge, Bernd Segnitz, Klemens Wild and Irmgard Sinning, 2017, 12, Text txt rdacontent, Computermedien c rdamedia, Online-Ressource cr rdacarrier, Published online 28 November 2016, Gesehen am 11.09.2018, Co-translational protein targeting and membrane protein insertion is a fundamental process and depends on the signal recognition particle (SRP). In mammals, SRP is composed of the SRP RNA crucial for SRP assembly and function and six proteins. The two largest proteins SRP68 and SRP72 form a heterodimer and bind to a regulatory site of the SRP RNA. Despite their essential roles in the SRP pathway, structural information has been available only for the SRP68 RNA-binding domain (RBD). Here we present the crystal structures of the SRP68 protein-binding domain (PBD) in complex with SRP72-PBD and of the SRP72-RBD bound to the SRP S domain (SRP RNA, SRP19 and SRP68) detailing all interactions of SRP72 within SRP. The SRP72-PBD is a tetratricopeptide repeat, which binds an extended linear motif of SRP68 with high affinity. The SRP72-RBD is a flexible peptide crawling along the 5e- and 5f-loops of SRP RNA. A conserved tryptophan inserts into the 5e-loop forming a novel type of RNA kink-turn stabilized by a potassium ion, which we define as K+-turn. In addition, SRP72-RBD remodels the 5f-loop involved in ribosome binding and visualizes SRP RNA plasticity. Docking of the S domain structure into cryo-electron microscopy density maps reveals multiple contact sites between SRP68/72 and the ribosome, and explains the role of SRP72 in the SRP pathway., Lapouge, Karine VerfasserIn (DE-588)1166462900 (DE-627)1030438048 (DE-576)510785050 aut, Segnitz, Bernd VerfasserIn (DE-588)1166674983 (DE-627)1030546207 (DE-576)510844332 aut, Wild, Klemens VerfasserIn (DE-588)1049291190 (DE-627)781602394 (DE-576)177410892 aut, Sinning, Irmgard 1960- VerfasserIn (DE-588)1027598617 (DE-627)72945133X (DE-576)166290580 aut, Enthalten in Nucleic acids research Oxford : Oxford Univ. Press, 1974 45(2017), 1, Seite 470-481 Online-Ressource (DE-627)26813250X (DE-600)1472175-2 (DE-576)07760878X 1362-4962 nnns, volume:45 year:2017 number:1 pages:470-481 extent:12, http://dx.doi.org/10.1093/nar/gkw1124 Verlag Resolving-System kostenfrei Volltext, https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5224484/ Verlag kostenfrei Volltext, http://dx.doi.org/10.1093/nar/gkw1124 LFER, LFER 2018-09-13T00:00:00Z |
| spellingShingle | Becker, Matthias Michael Markus, Lapouge, Karine, Segnitz, Bernd, Wild, Klemens, Sinning, Irmgard, Structures of human SRP72 complexes provide insights into SRP RNA remodeling and ribosome interaction, Co-translational protein targeting and membrane protein insertion is a fundamental process and depends on the signal recognition particle (SRP). In mammals, SRP is composed of the SRP RNA crucial for SRP assembly and function and six proteins. The two largest proteins SRP68 and SRP72 form a heterodimer and bind to a regulatory site of the SRP RNA. Despite their essential roles in the SRP pathway, structural information has been available only for the SRP68 RNA-binding domain (RBD). Here we present the crystal structures of the SRP68 protein-binding domain (PBD) in complex with SRP72-PBD and of the SRP72-RBD bound to the SRP S domain (SRP RNA, SRP19 and SRP68) detailing all interactions of SRP72 within SRP. The SRP72-PBD is a tetratricopeptide repeat, which binds an extended linear motif of SRP68 with high affinity. The SRP72-RBD is a flexible peptide crawling along the 5e- and 5f-loops of SRP RNA. A conserved tryptophan inserts into the 5e-loop forming a novel type of RNA kink-turn stabilized by a potassium ion, which we define as K+-turn. In addition, SRP72-RBD remodels the 5f-loop involved in ribosome binding and visualizes SRP RNA plasticity. Docking of the S domain structure into cryo-electron microscopy density maps reveals multiple contact sites between SRP68/72 and the ribosome, and explains the role of SRP72 in the SRP pathway. |
| swb_id_str | 510844391 |
| title | Structures of human SRP72 complexes provide insights into SRP RNA remodeling and ribosome interaction |
| title_auth | Structures of human SRP72 complexes provide insights into SRP RNA remodeling and ribosome interaction |
| title_full | Structures of human SRP72 complexes provide insights into SRP RNA remodeling and ribosome interaction Matthias M.M. Becker, Karine Lapouge, Bernd Segnitz, Klemens Wild and Irmgard Sinning |
| title_fullStr | Structures of human SRP72 complexes provide insights into SRP RNA remodeling and ribosome interaction Matthias M.M. Becker, Karine Lapouge, Bernd Segnitz, Klemens Wild and Irmgard Sinning |
| title_full_unstemmed | Structures of human SRP72 complexes provide insights into SRP RNA remodeling and ribosome interaction Matthias M.M. Becker, Karine Lapouge, Bernd Segnitz, Klemens Wild and Irmgard Sinning |
| title_in_hierarchy | Structures of human SRP72 complexes provide insights into SRP RNA remodeling and ribosome interaction / Matthias M.M. Becker, Karine Lapouge, Bernd Segnitz, Klemens Wild and Irmgard Sinning, |
| title_short | Structures of human SRP72 complexes provide insights into SRP RNA remodeling and ribosome interaction |
| title_sort | structures of human srp72 complexes provide insights into srp rna remodeling and ribosome interaction |
| url | http://dx.doi.org/10.1093/nar/gkw1124, https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5224484/ |