{"id":899,"date":"2018-05-23T15:49:43","date_gmt":"2018-05-23T19:49:43","guid":{"rendered":"https:\/\/research.cbc.osu.edu\/gopalan.5\/?page_id=899"},"modified":"2023-01-04T15:48:24","modified_gmt":"2023-01-04T20:48:24","slug":"rnase-p","status":"publish","type":"page","link":"https:\/\/research.cbc.osu.edu\/gopalan.5\/publications\/rnase-p\/","title":{"rendered":"RNase P"},"content":{"rendered":"

RNase P Publications<\/strong><\/h2>\n
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*Corresponding author(s)<\/p>\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n
Phan H-D\u00b0, Norris A\u00b0, Du C, Stachowski K, Khairunisa B, Sidharthan V, Mukhopadhyay B, Foster MP, Wysocki VH*, and Gopalan V*. (2022) Elucidation of structure-function relationships in Methanocaldococcus jannaschii RNase P, a multi-subunit catalytic ribonucleoprotein. Nucleic Acids Res.<\/em>, 50<\/strong>: 8154-8167 \u00b0joint first authors<\/em><\/strong><\/td>\n<\/td>\n<\/tr>\n
Lai LB, Lai SM, Szymanski ES, Kapur M, Choi EK, Al-Hashimi HM, Ackerman SL*, and Gopalan V*. (2022) Structural basis for impaired 5\u2032 processing of a mutant tRNA associated with defects in neuronal homeostasis. PNAS<\/em>, 119<\/strong>: e2119529119.<\/td>\n<\/td>\n<\/tr>\n
Phan H-D, Lai LB*, Zahurancik WJ, and Gopalan V*. (2021) The many faces of RNA-based RNase P: An RNA-world relic. Trends Biochem. Sci.<\/em>, 46<\/strong>: 976-991.<\/td>\n<\/td>\n<\/tr>\n
Marathe IA, Lai SM\u00b0, Zahurancik WJ\u00b0, Poirier MG, Wysocki VH, and Gopalan V*. (2021) Protein cofactors and substrate dictate Mg2+-dependent structural changes in the catalytic RNA of archaeal RNase P. Nucleic Acids Res.<\/em>, 49<\/strong>: 9444-9458. \u00b0joint second authors<\/em><\/strong><\/td>\n<\/td>\n<\/tr>\n
Zahurancik WJ, Norris AS, Lai SB, Snyder DT, Wysocki VH*, and Gopalan V*. (2021) Purification, reconstitution, and mass analysis of archaeal RNase P, a multi-subunit ribonucleoprotein enzyme. Methods Enzymol.<\/em>, 659<\/strong>: 71-103.<\/td>\n<\/td>\n<\/tr>\n
Lai SM and Gopalan V*. (2021) Using an L7Ae-tethered, hydroxyl radical-mediated footprinting strategy to identify and validate kink-turns in RNAs. Methods Mol. Biol.<\/em>, 2167<\/strong>: 147-69.<\/td>\n<\/td>\n<\/tr>\n
Li W, Xiong Y, Lai LB, Zhang K, Li Z, Kang H, Dai L, Gopalan V*, Wang G-L*, and Liu W* (2021) The rice RNase P protein subunit Rpp30 confers broad-spectrum resistance to fungal and bacterial pathogens. Plant Biotechnol. J.<\/em>, 19<\/strong>: 1988-1999<\/td>\n<\/td>\n<\/tr>\n
Yu AM, Gaspar P, Cheng L, Lai LB, Kaur S, Gopalan V, Chen AA*, and Lucks JB* (2021) Computationally reconstructing co-transcriptional RNA folding pathways from experimental data reveals rearrangement of non-native folding intermediates. Mol. Cell<\/em>, 81<\/strong>: 870-883.<\/td>\n<\/td>\n<\/tr>\n
Lai LB, Phan H-D, Zahurancik WJ, and Gopalan V* (2020) Alternative protein topology-mediated evolution of a catalytic ribonucleoprotein. Trends Biochem. Sci.<\/em>, 45: 825-828<\/strong>.<\/td>\n<\/td>\n<\/tr>\n
Gray MW* and Gopalan V*. (2020) Piece by piece: Building a ribozyme.\u00a0J. Biol. Chem.<\/em>, 295<\/strong>: 2313-2323.<\/td>\n<\/td>\n<\/tr>\n
Palsule G, Gopalan V, and Simcox A*. (2019) Biogenesis of RNase P RNA from an intron requires co-assembly with cognate protein subunits. Nucleic Acids Res.<\/em>, 47<\/strong>: 8746-8754.<\/a> [SI<\/a>]<\/td>\n<\/td>\n<\/tr>\n
Daniels CJ*, Lai LB, Chen T-H, and Gopalan V. (2019) Both kinds of RNase P in all domains of life: Surprises galore. RNA<\/em>, 25<\/strong>: 286-291.<\/a><\/td>\n<\/td>\n<\/tr>\n
Chen T-H, Sotomayor M, and Gopalan V*. (2019) Biochemical studies provide insights into the necessity for multiple Arabidopsis thaliana<\/em> protein-only RNase P isoenzymes. J. Mol. Biol.<\/em>, 431<\/strong>: 615-624.<\/td>\n<\/td>\n<\/tr>\n
Gopalan V*, Jarrous N*, and Krasilnikov AS*. (2018) Chance and necessity in the evolution of RNase P. RNA<\/em>, 24<\/strong>: 1-5.<\/td>\n<\/td>\n<\/tr>\n
Lai LB*, Tanimoto A^, Lai SM^, Chen W-Y, Marathe IA, Westhof E, Wysocki VH, and Gopalan V*. (2017) A novel double kink-turn module in euryarchaeal RNase P RNAs. Nucleic Acids Res.<\/em>, 45<\/strong>: 7432-7440.<\/a> [SI<\/a>] ^joint second authors<\/em><\/strong><\/td>\n<\/td>\n<\/tr>\n
Mao G\u00b0, Chen T-H\u00b0, Srivastava AS, Kosek D, Biswas PK, Gopalan V, and Kirsebom LA*. (2016) Cleavage of model substrates by Arabidopsis thaliana<\/em> PRORP1 reveals new insights into its substrate requirements. PLoS ONE<\/em>, 11<\/strong>: e0160246.<\/a> [SI<\/a>] \u00b0joint first authors<\/em><\/strong><\/td>\n<\/td>\n<\/tr>\n
Chen T-H, Tanimoto A, Shkriabai N, Kvaratskhelia M, Wysocki V*, and Gopalan V*. (2016) Use of chemical modification and mass spectrometry to identify substrate-contacting sites in proteinaceous RNase P, a tRNA processing enzyme. Nucleic Acids Res.<\/em>, 44<\/strong>: 5344-5355.<\/a> [SI<\/a>]<\/td>\n<\/td>\n<\/tr>\n
Samanta MP\u00b0*, Lai SM\u00b0, Daniels CJ, and Gopalan V*. (2016) Sequence analysis and comparative study of the protein subunits of archaeal RNase P. Biomolecules<\/em>, 6<\/strong>: 22.<\/a> [SI<\/a>] \u00b0joint first authors<\/em><\/strong><\/td>\n<\/td>\n<\/tr>\n
Manivannan SN, Lai LB, Gopalan V*, and Simcox A*. (2015) Transcriptional control of an essential ribozyme in Drosophila<\/em> reveals an ancient evolutionary divide in animals. PLoS Genet.<\/em>, 11<\/strong>: e1004893.<\/a> [SI 1<\/a>, 2<\/a>]<\/td>\n<\/td>\n<\/tr>\n
Lai SM, Lai LB, Foster MP*, and Gopalan V*. (2014) The L7Ae protein binds to two kink-turns in the Pyrococcus furiosus<\/em> RNase P RNA. Nucleic Acids Res.<\/em>, 42<\/strong>: 13328-13338.<\/a> [SI<\/a>]<\/td>\n<\/td>\n<\/tr>\n
Ma X\u00b0, Lai LB\u00b0, Lai SM\u00b0, Tanimoto A, Foster MP, Wysocki VH*, and Gopalan V*. (2014) Uncovering the stoichiometry of Pyrococcus furiosus<\/em> RNase P, a multi-subunit catalytic ribonucleoprotein complex, by surface-induced dissociation and ion mobility mass spectrometry. Angew. Chem. Int. Ed. Engl.<\/em>, 53<\/strong>: 11483-11487.<\/a> [SI<\/a>] \u00b0joint first authors<\/em><\/strong><\/td>\n<\/td>\n<\/tr>\n
Susanti D, Johnson EF, Rodriguez JR, Anderson I, Perevalova AA, Kyrpides N, Lucas S, Han J, Lapidus A, Cheng J-F, Goodwin L, Pitluck S, Mavrommatis K, Peters L, Land ML, Hauser L, Gopalan V, Chan PP, Lowe TM, Atomi H, Bonch-Osmolovskaya EA, Woyke T, and Mukhopadhyay B*. (2012) Complete genome sequence of Desulfurococcus fermentans<\/em>, a hyperthermophilic cellulolytic crenarchaeon isolated from a freshwater hot spring in Kamchatka, Russia. J. Bacteriol.<\/em>, 194<\/strong>: 5703-5704.<\/a><\/td>\n<\/td>\n<\/tr>\n
Xu Y, Oruganti SV, Gopalan V, and Foster MP*. (2012) Thermodynamics of coupled folding in the interaction of archaeal RNase P proteins RPP21 and RPP29. Biochemistry<\/em>, 51<\/strong>: 926-935.<\/a> [SI<\/a>]<\/td>\n<\/td>\n<\/tr>\n
Chen W-Y, Singh D, Lai LB, Stiffler MA, Lai HD, Foster MP, and Gopalan V*. (2012) Fidelity of tRNA 5\u2032-maturation: a possible basis for the functional dependence of archaeal and eukaryal RNase P on multiple protein cofactors. Nucleic Acids Res.<\/em>, 40<\/strong>: 4666-4680.<\/a> [SI<\/a>]<\/td>\n<\/td>\n<\/tr>\n
Crowe BL, Bohlen CJ, Wilson RC, Gopalan V, and Foster MP*. (2011) Assembly of the complex between archaeal RNase P proteins RPP30 and Pop5. Archaea<\/em>, doi:10.1155\/2011\/891531.<\/a><\/td>\n<\/td>\n<\/tr>\n
Lai LB, Bernal-Bayard P, Mohannath G, Lai SM, Gopalan V*, and Vioque A*. (2011) A functional RNase P protein subunit of bacterial origin in some eukaryotes. Mol. Genet. Genomics<\/em>, 286<\/strong>: 359-369.<\/td>\n<\/td>\n<\/tr>\n
Sinapah S\u00b0, Wu S\u00b0, Chen Y\u00b0, Pettersson BMF, Gopalan V, and Kirsebom LA*. (2011) Cleavage of model substrates by archaeal RNase P: role of protein cofactors in cleavage-site selection. Nucleic Acids Res.<\/em>, 39<\/strong>: 1105-1116.<\/a> [SI<\/a>] \u00b0joint first authors<\/em><\/strong><\/td>\n<\/td>\n<\/tr>\n
Cho I-M, Kazakov SA, and Gopalan V*. (2011) Evidence for recycling of external guide sequences during cleavage of bipartite substrates in vitro<\/em> by reconstituted archaeal RNase P. J. Mol. Biol.<\/em>, 405<\/strong>: 1121-1127.<\/a> [SI<\/a>]<\/td>\n<\/td>\n<\/tr>\n
Chen W-Y\u00b0, Xu Y\u00b0, Cho I-M, Oruganti SV, Foster MP*, and Gopalan V*. (2011) Cooperative RNP assembly: complementary rescue of structural defects by protein and RNA subunits of archaeal RNase P. J. Mol. Biol.<\/em>, 411<\/strong>: 368-383.<\/a> \u00b0joint first authors<\/em><\/strong><\/td>\n<\/td>\n<\/tr>\n
Chen W-Y\u00b0, Pulukkunat DK\u00b0, Cho I-M, Tsai H-Y, and Gopalan V*. (2010) Dissecting functional cooperation among protein subunits in archaeal RNase P, a catalytic ribonucleoprotein complex. Nucleic Acids Res.<\/em>, 38<\/strong>: 8316-8327.<\/a> [SI<\/a>] \u00b0joint first authors<\/em><\/strong><\/td>\n<\/td>\n<\/tr>\n
Jarrous N* and Gopalan V. (2010) Archaeal\/Eukaryal RNase P: subunits, functions, and RNA diversification. Nucleic Acids Res.<\/em>, 38<\/strong>: 7885-7894.<\/a> [SI<\/a>] (Highlighted as a featured article)<\/em><\/strong><\/td>\n<\/td>\n<\/tr>\n
Lai LB\u00b0, Chan PP\u00b0, Cozen AE, Bernick DL, Brown JW, Gopalan V*, and Lowe TM*. (2010) Discovery of a minimal form of RNase P in Pyrobaculum<\/em>. Proc. Natl. Acad. Sci. USA<\/em>, 107<\/strong>: 22493-22498.<\/a> [SI<\/a>] (Highlighted on the cover and in a commentary)<\/em><\/strong> \u00b0joint first authors<\/em><\/strong><\/td>\n<\/td>\n<\/tr>\n
Cho I-M, Lai LB, Susanti D, Mukhopadhyay B, and Gopalan V*. (2010) Ribosomal protein L7Ae is a subunit of archaeal RNase P. Proc. Natl. Acad. Sci. USA<\/em>, 107<\/strong>: 14573-14578.<\/a> [SI<\/a>]<\/td>\n<\/td>\n<\/tr>\n
Lai LB, Cho I-M, Chen W-Y, and Gopalan V*. (2010) Archaeal RNase P: a mosaic of its bacterial and eukaryal relatives. In F Liu and S Altman (Eds.), Ribonuclease P<\/em> (Protein Reviews, vol. 10; pp. 153-172). New York, NY: Springer Science + Business Media, LLC.<\/td>\n<\/td>\n<\/tr>\n
McClain WH*, Lai LB, and Gopalan V. (2010) Trials, travails, and triumphs: an account of RNA catalysis in RNase P. J. Mol. Biol.<\/em>, 397<\/strong>: 627-646.<\/td>\n<\/td>\n<\/tr>\n
Lai LB, Vioque A, Kirsebom LA*, and Gopalan V*. (2010) Unexpected diversity of RNase P, an ancient tRNA processing enzyme: challenges and prospects. FEBS Lett.<\/em>, 584<\/strong>: 287-296.<\/a> (Invited article for a special issue)<\/em><\/strong><\/td>\n<\/td>\n<\/tr>\n
Xu Y, Amero CD^, Pulukkunat DK^, Gopalan V*, and Foster MP*. (2009) Solution structure of an archaeal RNase P binary protein complex: Formation of the 30-kDa complex between Pyrococcus furiosus<\/em> RPP21 and RPP29 is accompanied by coupled protein folding and highlights critical features for protein\u2013protein and protein\u2013RNA interactions. J. Mol. Biol.<\/em>, 393<\/strong>: 1043-1055.<\/a> [SI<\/a>] (Highlighted on the cover)<\/em><\/strong> ^joint second authors<\/em><\/strong><\/td>\n<\/td>\n<\/tr>\n
Pulukkunat DK and Gopalan V*. (2008) Studies on Methanocaldococcus jannaschii<\/em> RNase P reveal insights into the roles of RNA and protein cofactors in RNase P catalysis. Nucleic Acids Res.<\/em>, 36<\/strong>: 4172-4180.<\/a> [SI<\/a>]<\/td>\n<\/td>\n<\/tr>\n
Kawamoto SA\u00b0, Sudhahar CG\u00b0, Hatfield CL\u00b0, Sun J, Behrman EJ, and Gopalan V*. (2008) Studies on the mechanism of inhibition of bacterial ribonuclease P by aminoglycoside derivatives. Nucleic Acids Res.<\/em>, 36<\/strong>: 697-704.<\/a> [SI<\/a>] \u00b0joint first authors<\/em><\/strong><\/td>\n<\/td>\n<\/tr>\n
Gopalan V*. (2007) Uniformity amid diversity in RNase P. Proc. Natl. Acad. Sci. USA<\/em>, 104<\/strong>: 2031-2032.<\/a><\/td>\n<\/td>\n<\/tr>\n
Gopalan V and Altman S*. (2007) Ribonuclease P: structure and catalysis. In RF Gesteland, TR Cech, and JF Atkins (Eds.), The RNA World<\/em> (3rd edition; online version only). New York, NY: Cold Spring Harbor Laboratory Press.<\/a><\/td>\n<\/td>\n<\/tr>\n
Tsai H-Y, Pulukkunat DK, Woznick WK, and Gopalan V*. (2006) Functional reconstitution and characterization of Pyrococcus furiosus<\/em> RNase P. Proc. Natl. Acad. Sci. USA<\/em>, 103<\/strong>: 16147-16152.<\/a> [SI<\/a>]<\/td>\n<\/td>\n<\/tr>\n
Rangarajan S, Stephen Raj ML, Hernandez JM, Grotewold E, and Gopalan V*. (2004) RNase P as a tool for disruption of gene expression in maize cells. Biochem. J.<\/em>, 380<\/strong>: 611-616.<\/a><\/td>\n<\/td>\n<\/tr>\n
Gopalan V, Vioque A, and Altman S*. (2004) RNase P: variations and uses. In E Keinan, I Schechter, and M Sela (Eds.), Life Sciences for the 21st Century<\/em>, (pp. 49-59). Weinheim, Germany: Wiley-VCH.<\/td>\n<\/td>\n<\/tr>\n
Boomershine WP, McElroy CA, Tsai H-Y, Wilson RC, Gopalan V, and Foster MP*. (2003) Structure of Mth11\/Mth<\/em> Rpp29, an essential protein subunit of archaeal and eukaryotic RNase P. Proc. Natl. Acad. Sci. USA<\/em>, 100<\/strong>: 15398-15403.<\/a><\/td>\n<\/td>\n<\/tr>\n
Eder PS, Hatfield C, Vioque A, and Gopalan V*. (2003) Bacterial RNase P as a potential target for novel anti-infectives. Curr. Opin. Investig. Drugs<\/em>, 4<\/strong>: 937-943.<\/td>\n<\/td>\n<\/tr>\n
Boomershine WP, Stephen Raj ML, Gopalan V, and Foster MP*. (2003) Preparation of uniformly labeled NMR samples in Escherichia coli<\/em> under the tight control of the araBAD<\/em> promoter: expression of an archaeal homolog of the RNase P Rpp29 protein. Protein Expr. Purif.<\/em>, 28<\/strong>: 246-251.<\/td>\n<\/td>\n<\/tr>\n
Pulukkunat DK, Stephen Raj ML, Pattanayak D, Lai LB, and Gopalan V*. (2003) Exploring the potential of plant RNase P as a functional genomics tool. In E. Grotewold (Ed.), Plant Functional Genomics<\/em> (Methods in Molecular Biology, vol. 236; pp. 295-309). Totowa, NJ: Humana Press, Inc.<\/td>\n<\/td>\n<\/tr>\n
Tsai H-Y, Masquida B, Biswas R, Westhof E, and Gopalan V*. (2003) Molecular modeling of the three-dimensional structure of the bacterial RNase P holoenzyme. J. Mol. Biol.<\/em>, 325<\/strong>: 661-675.<\/td>\n<\/td>\n<\/tr>\n
Jovanovic M, Sanchez R, Altman S, and Gopalan V*. (2002) Elucidation of structure\u2013function relationships in the protein subunit of bacterial RNase P using a genetic complementation approach. Nucleic Acids Res.<\/em>, 30<\/strong>: 5065-5073.<\/a> [SI<\/a>]<\/td>\n<\/td>\n<\/tr>\n
Eubank TD, Biswas R, Jovanovic M, Litovchick A, Lapidot A, and Gopalan V*. (2002) Inhibition of bacterial RNase P by aminoglycoside\u2013arginine conjugates. FEBS Lett.<\/em>, 511<\/strong>: 107-112.<\/a><\/td>\n<\/td>\n<\/tr>\n
Guerrier-Takada C, Eder PS, Gopalan V, and Altman S*. (2002) Purification and characterization of Rpp25, an RNA-binding protein subunit of human ribonuclease P. RNA<\/em>, 8<\/strong>: 290-295.<\/a><\/td>\n<\/td>\n<\/tr>\n
Gopalan V, Vioque A, and Altman S*. (2002) RNase P: variations and uses. J. Biol. Chem.<\/em>, 277<\/strong>: 6759-6762.<\/a><\/td>\n<\/td>\n<\/tr>\n
Stephen Raj ML, Pulukkunat DK, Reckard JF III, Thomas G, and Gopalan V*. (2001) Cleavage of bipartite substrates by rice and maize ribonuclease P. Application to degradation of target mRNAs in plants. Plant Physiol.<\/em>, 125<\/strong>: 1187-1190.<\/a><\/td>\n<\/td>\n<\/tr>\n
Altman S*, Gopalan V, and Vioque A. (2000) Varieties of RNase P: a nomenclature problem? RNA<\/em>, 6<\/strong>: 1689-1694.<\/a><\/td>\n<\/td>\n<\/tr>\n
Biswas R, Ledman DW, Fox RO, Altman S, and Gopalan V*. (2000) Mapping RNA-protein interactions in ribonuclease P from Escherichia coli<\/em> using disulfide-linked EDTA-Fe. J. Mol. Biol.<\/em>, 296<\/strong>: 19-31.<\/td>\n<\/td>\n<\/tr>\n
Gopalan V*, K\u00fchne H, Biswas R, Li H, Brudvig GW, and Altman S. (1999) Mapping RNA\u2013protein interactions in ribonuclease P from Escherichia coli<\/em> using electron paramagnetic resonance spectroscopy. Biochemistry<\/em>, 38<\/strong>: 1705-1714.<\/td>\n<\/td>\n<\/tr>\n<\/tbody>\n<\/table>\n","protected":false},"excerpt":{"rendered":"

RNase P Publications *Corresponding author(s) Phan H-D\u00b0, Norris A\u00b0, Du C, Stachowski K, Khairunisa B, Sidharthan V, Mukhopadhyay B, Foster MP, Wysocki VH*, and Gopalan V*. (2022) Elucidation of structure-function relationships in Methanocaldococcus jannaschii RNase P, a multi-subunit catalytic ribonucleoprotein. Nucleic Acids Res., 50: 8154-8167 \u00b0joint first authors Lai LB, Lai SM, Szymanski ES, Kapur […]<\/p>\n","protected":false},"author":9,"featured_media":0,"parent":177,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"_exactmetrics_skip_tracking":false,"_exactmetrics_sitenote_active":false,"_exactmetrics_sitenote_note":"","_exactmetrics_sitenote_category":0,"footnotes":""},"class_list":["post-899","page","type-page","status-publish","hentry","post-preview"],"jetpack_shortlink":"https:\/\/wp.me\/P8Lmk8-ev","jetpack_sharing_enabled":true,"_links":{"self":[{"href":"https:\/\/research.cbc.osu.edu\/gopalan.5\/wp-json\/wp\/v2\/pages\/899","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/research.cbc.osu.edu\/gopalan.5\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/research.cbc.osu.edu\/gopalan.5\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/research.cbc.osu.edu\/gopalan.5\/wp-json\/wp\/v2\/users\/9"}],"replies":[{"embeddable":true,"href":"https:\/\/research.cbc.osu.edu\/gopalan.5\/wp-json\/wp\/v2\/comments?post=899"}],"version-history":[{"count":25,"href":"https:\/\/research.cbc.osu.edu\/gopalan.5\/wp-json\/wp\/v2\/pages\/899\/revisions"}],"predecessor-version":[{"id":2127,"href":"https:\/\/research.cbc.osu.edu\/gopalan.5\/wp-json\/wp\/v2\/pages\/899\/revisions\/2127"}],"up":[{"embeddable":true,"href":"https:\/\/research.cbc.osu.edu\/gopalan.5\/wp-json\/wp\/v2\/pages\/177"}],"wp:attachment":[{"href":"https:\/\/research.cbc.osu.edu\/gopalan.5\/wp-json\/wp\/v2\/media?parent=899"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}