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| | ==Crystal structure of NN domain of resistance protein== | | ==Crystal structure of NN domain of resistance protein== |
| - | <StructureSection load='3wrv' size='340' side='right' caption='[[3wrv]], [[Resolution|resolution]] 2.75Å' scene=''> | + | <StructureSection load='3wrv' size='340' side='right'caption='[[3wrv]], [[Resolution|resolution]] 2.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3wrv]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WRV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WRV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3wrv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Solanum_lycopersicum Solanum lycopersicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WRV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WRV FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vkw|3vkw]], [[3wrw|3wrw]], [[3wrx|3wrx]], [[3wry|3wry]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wrv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wrv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wrv RCSB], [http://www.ebi.ac.uk/pdbsum/3wrv PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3wrv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wrv OCA], [https://pdbe.org/3wrv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wrv RCSB], [https://www.ebi.ac.uk/pdbsum/3wrv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wrv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/TM1R_SOLLC TM1R_SOLLC] Inhibitor of viral RNA replication which confers resistance to some tobamoviruses including tomato mosaic virus (ToMV) (e.g. isolate L), tobacco mosaic virus (TMV), tobacco mild green mosaic virus (TMGMV) and pepper mild mottle virus (PMMoV), but not to resistance-breaking isolates of ToMV (e.g. LT1, SL-1 and ToMV1-2) and tomato brown rugose fruit virus (ToBRFV) (PubMed:17699618, PubMed:3686829, PubMed:17238011, PubMed:19423673, PubMed:23415925, PubMed:29582165, PubMed:28107419). Prevents tobamoviruses RNA replication by affecting the association of tobamoviruses replication proteins (large and small subunits) with host membrane-associated proteins (e.g. TOM1, TOM2A and ARL8), thus inhibiting the replication complex formation on the membranes and avoiding viral negative-strand RNA synthesis (PubMed:17699618, PubMed:19423673, PubMed:23658455, PubMed:23415925). Inhibits triphosphatase activity of ToMV replication proteins (PubMed:25092327).<ref>PMID:17238011</ref> <ref>PMID:17699618</ref> <ref>PMID:19423673</ref> <ref>PMID:23415925</ref> <ref>PMID:23658455</ref> <ref>PMID:25092327</ref> <ref>PMID:28107419</ref> <ref>PMID:29582165</ref> <ref>PMID:3686829</ref> |
| - | Tm-1, the protein product of Tm-1, a semidominant resistance gene of tomato, inhibits tomato mosaic virus (ToMV) replication by binding to ToMV replication proteins. Previous studies suggested the importance of the Tm-1 N-terminal region for its inhibitory activity; however, it has not been determined if the N-terminal region is sufficient for inhibition. Furthermore, the three-dimensional structure of Tm-1 has not been determined. In this study, an N-terminal fragment of Tm-1 (residues 1-431) as a fusion protein containing an upstream maltose-binding protein was expressed in E. coli Rosetta (DE3) cells at 30 degrees C and then purified. The solubility of the fusion protein was greater when the cells were cultured at 30 degrees C than when cultured at lower or higher temperatures. The purified N-terminal Tm-1 fragment from which the maltose-binding protein tag had been removed has inhibitory activity against ToMV RNA replication.
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| - | Expression, purification, and functional characterization of an N-terminal fragment of the tomato mosaic virus resistance protein Tm-1.,Kato M, Ishibashi K, Kobayashi C, Ishikawa M, Katoh E Protein Expr Purif. 2013 May;89(1):1-6. doi: 10.1016/j.pep.2013.02.001. Epub 2013, Feb 13. PMID:23415925<ref>PMID:23415925</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div> | + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Katoh, E]] | + | [[Category: Large Structures]] |
| - | [[Category: Matsumura, H]] | + | [[Category: Solanum lycopersicum]] |
| - | [[Category: Alpha/beta domain]] | + | [[Category: Katoh E]] |
| - | [[Category: Resistance]] | + | [[Category: Matsumura H]] |
| - | [[Category: Transferase]]
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| Structural highlights
Function
TM1R_SOLLC Inhibitor of viral RNA replication which confers resistance to some tobamoviruses including tomato mosaic virus (ToMV) (e.g. isolate L), tobacco mosaic virus (TMV), tobacco mild green mosaic virus (TMGMV) and pepper mild mottle virus (PMMoV), but not to resistance-breaking isolates of ToMV (e.g. LT1, SL-1 and ToMV1-2) and tomato brown rugose fruit virus (ToBRFV) (PubMed:17699618, PubMed:3686829, PubMed:17238011, PubMed:19423673, PubMed:23415925, PubMed:29582165, PubMed:28107419). Prevents tobamoviruses RNA replication by affecting the association of tobamoviruses replication proteins (large and small subunits) with host membrane-associated proteins (e.g. TOM1, TOM2A and ARL8), thus inhibiting the replication complex formation on the membranes and avoiding viral negative-strand RNA synthesis (PubMed:17699618, PubMed:19423673, PubMed:23658455, PubMed:23415925). Inhibits triphosphatase activity of ToMV replication proteins (PubMed:25092327).[1] [2] [3] [4] [5] [6] [7] [8] [9]
References
- ↑ Strasser M, Pfitzner AJ. The double-resistance-breaking Tomato mosaic virus strain ToMV1-2 contains two independent single resistance-breaking domains. Arch Virol. 2007;152(5):903-14. PMID:17238011 doi:10.1007/s00705-006-0915-8
- ↑ Ishibashi K, Masuda K, Naito S, Meshi T, Ishikawa M. An inhibitor of viral RNA replication is encoded by a plant resistance gene. Proc Natl Acad Sci U S A. 2007 Aug 21;104(34):13833-8. PMID:17699618 doi:10.1073/pnas.0703203104
- ↑ Ishibashi K, Naito S, Meshi T, Ishikawa M. An inhibitory interaction between viral and cellular proteins underlies the resistance of tomato to nonadapted tobamoviruses. Proc Natl Acad Sci U S A. 2009 May 26;106(21):8778-83. PMID:19423673 doi:10.1073/pnas.0809105106
- ↑ Kato M, Ishibashi K, Kobayashi C, Ishikawa M, Katoh E. Expression, purification, and functional characterization of an N-terminal fragment of the tomato mosaic virus resistance protein Tm-1. Protein Expr Purif. 2013 May;89(1):1-6. doi: 10.1016/j.pep.2013.02.001. Epub 2013, Feb 13. PMID:23415925 doi:http://dx.doi.org/10.1016/j.pep.2013.02.001
- ↑ Ishibashi K, Ishikawa M. The resistance protein Tm-1 inhibits formation of a Tomato mosaic virus replication protein-host membrane protein complex. J Virol. 2013 Jul;87(14):7933-9. PMID:23658455 doi:10.1128/JVI.00743-13
- ↑ Ishibashi K, Kezuka Y, Kobayashi C, Kato M, Inoue T, Nonaka T, Ishikawa M, Matsumura H, Katoh E. Structural basis for the recognition-evasion arms race between Tomato mosaic virus and the resistance gene Tm-1. Proc Natl Acad Sci U S A. 2014 Aug 19;111(33):E3486-95. doi:, 10.1073/pnas.1407888111. Epub 2014 Aug 4. PMID:25092327 doi:http://dx.doi.org/10.1073/pnas.1407888111
- ↑ Luria N, Smith E, Reingold V, Bekelman I, Lapidot M, Levin I, Elad N, Tam Y, Sela N, Abu-Ras A, Ezra N, Haberman A, Yitzhak L, Lachman O, Dombrovsky A. A New Israeli Tobamovirus Isolate Infects Tomato Plants Harboring Tm-22 Resistance Genes. PLoS One. 2017 Jan 20;12(1):e0170429. PMID:28107419 doi:10.1371/journal.pone.0170429
- ↑ Maayan Y, Pandaranayaka EPJ, Srivastava DA, Lapidot M, Levin I, Dombrovsky A, Harel A. Using genomic analysis to identify tomato Tm-2 resistance-breaking mutations and their underlying evolutionary path in a new and emerging tobamovirus. Arch Virol. 2018 Jul;163(7):1863-1875. PMID:29582165 doi:10.1007/s00705-018-3819-5
- ↑ Watanabe Y, Kishibayashi N, Motoyoshi F, Okada Y. Characterization of Tm-1 gene action on replication of common isolates and a resistance-breaking isolate of TMV. Virology. 1987 Dec;161(2):527-32. PMID:3686829 doi:10.1016/0042-6822(87)90147-4
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