I’m looking for concise, clear science writing, like you’re writing up a synopsi
ID: 213965 • Letter: I
Question
I’m looking for concise, clear science writing, like you’re writing up a synopsis of this article or video for a scientific magazine: what are the major points here?, what’s new here to you?, what are the broad take-home messages (if any)? (Description of a good scientific paper synopsis here. I’m looking for something around 300-500 words per synopsis.) Please!
letters to nature 12. Chaier, G. etaThe tador tandam of S3BPl: srtaal motif involvad in DNA and RG-ridh cellular metabolism3. The 5 untranslated region of many mRNAs of genes involved in purine metabolism and transport contain a guanine-responsive riboswitch that directly binds guanine 14.Sprangen, R, Growes, M. R., Sinning. L &Santler;, M. High-rX-ry and NMR sructunes of hypoxanthine or xanthine to terminate transcription*. Here peptide binding Struchure 12, 1551-1962 (2004) 13.Selenko, P eal SMN udordomain aructure and its interaction with the Sm proteins. Nature Strct the SMNTador domin: confomational variationin the binding site for symmcaed we report the crystal structure at 1.95 A resolution of the arginine nsidues. Mal. Rial. 327, 507-520 (003). Am Rev oys Biamot Struct 32, 115-133 (2003) muscular ophy gene, binds prefentiallytodialaiine-containing protein targets Mal Gefl e-binding 15. Theobald, D.L. Mrtoo Fry, R M.&Wattke;, D.S. Nuclsic acid reco gnition by OB- fold protcins. xpt pbuX operon of B. subtilis bound to hypoxanthine, a preva- 16. Fniesen, W. L, Maenct, S, Paashlin, S, Wyce, A & Dryfs, G. SMN the prodact of the sent metabolite in the bacterial purine salvage pathway. This structure reveals a complex RNA fold involving several phylo- of genetically conserved nucleotides that create a binding pocket y envelops the ligand. Hypoxanthine func- tions to stabilize this structure and to promote the formation of a downstream transcriptional terminator element, thereby provid- 7, 1111-1117 (2001). 17. Brahms, H. Meeus, L, de Balar dere, V., Fischer, U. & Luhrmann, R. Symmetrical methylation argnine residues inliceokaal Sm protein BrB' and the Sm-like protein LSm4, and ther interaction with the SMN protein. RNA 7, 1531-1542 (201) 18. Kouzandes T. Histone methylat on in trusciptional contoL alOpie Genet. Des. 12, 196-209 s. 5eng Q, t al Matylation of HB bsine 79 is modiated by a newamilyas without a SET ing a mechanism for directly repressing gene expression in bind practically any imaginable ligand has been harnessed to 23. San-Sqgundo, P.A. & Ronder, G S.Role for the slming prosin Detl in meiotic chekpoint coatrol. able promise for real-life applications8. Yet, nature has preceded response to an increase in intracellular concentrations of domain. an". Biol, 12, 1052-1058 (2002), of the nuckosome core. Celf 109, 745-756 (2002), chromatin-speific histone H3 met hyltranferase.I Bid. Chem. 277, 30421-3042402) Saccharomyees deletion mutants that affect radiation sensitvty. Gentis online pubication, 15 20. van Leeuwen, E, Gaken, P.R. Gottachling.D. EDoipmoduates slncing inyeas bynacthylationmetabolite. 21. Lacoste, N., Utley, R.T, Hunter, L M., Poirier, GG&Cote;, J. Disruptor of tdomeric slencing 1 is a 22. GameLC, Witiamson M.S.& Baccri,C.X-scaacteristiks and genctic anabysi for nine engineer RNA-based biosensors and molecular machines that approaches hold r 2004 (doi:l esc 24. Rogakou E.P.Boon, C. Redon C& Bonner,W. M.Megbse hromatin domains invorve d in DNA called riboswitches, that directly control gene expression through their ability to bind various small-molecule metabolites2. These sensors are exemplified by the guanine-responsive riboswitch that 26. Celeste, A et al.Histone H2AX phosphoryation is dspensable for the initial recognition of DNA controls the transcription of genes associated with purine metabo- Mol. Biol ll 11, 3601-3615 (2000). double-tand breaks in véva. T. Cell Biol 146, 905-916 (1999) autophosphorylation and dimer dissociation. Natre 421, 499-506 (2003) breas. Neture Ce Biol 5, 675-679 (2003) 25. Ratkmit, G L & Kastan, M.B. DNA damage activates ATM through intermolecular secon 27. Luger, K, Mader, A. V. Richmond R K.·Sargent. D. R & Richmond. TL Crystal structure of the structure of this motif consists of three helices (PI-P3) that 28. Mozziconacd. I & Vicor, L M. Nadeosome gapa functional stractuor the 30nm surround a three-way junction (Fig. la), with phylogenetically conserved nucleotides located in the junction and loops. Immedi LS the switching domain (Fig. 1b), which has been proposed to control monoubiquitinated PCNA: a pas ble mchanism for the polymerase with in rsponse to DNA geneexpression by forming either a terminator or an antiterminator Nature 389, 251-260(1997). chromatin fiber. J. Sruct Bial 143, 72-76 (2003) 29. Hyen, Y et al Sructural differences in the DNA binding domains of haman p33 and its C elegans 0 ne ortholog Cep1.Stuae 12, 1237-1243 0. Kannouche, P.L. Wing J&Lehmann;, A. R. Interaction ofhaman DNA polymerase e with damage. Mol. Cel 14,491-500 (2004) element, depending on whether metabolite is bound" sensor solved by X-ray crys tallography the structure of the guanine binding domain bound to hypoxanthine (Supplementary Table SI support and discussion the Wistar Instituse Proteomics Faciliy (K. Speicher) for prosein and Supplementary Fig. SI), a biologically relevant ligand of the Acknowiedgements The authors thank N. Pavletich, S. Barger, G. Dreyfuss and R Kaufman for guan the RNA xanthine-bound state, N-tarminal sequencing and mass spectrometry analysis, and the University of ennsylvania Protein Chemistry Facility Lambris and M. Katragadda) for calori netry analysis. This work was supported by a grant to TD.H. from the National Cancer Institute nine ve adopts a three-dimensional fold in which the terminal loops (1.2 and L3) form a series of interconnecting hydrogen bonds (see pairing scheme in Fig. la) to bring the P2 and P3 helices parallel to each other (Fig. 1c, d). Unfavourable electrostatic interactions, a Competing interests statement The authors daclare that they have no competing hnancial ition of regions of the ribose-phosphate Correspondence and roquests for materias should be addresed toTDH. (halanonetis@wistar.upenn edu). Structure coordinates have been deposited in the Protein Data Bank under the accession code IXNI in between the two backbones (Supplementary Fig. S2). Anchoring the global helical arrangement of the RNA are numerous tertiary ina loop (Fig. lc) interacting with bound hypoxanthine, the Pl helix, and the J1/2 and J3/1 loops. The purine-binding pocket is created by conserved nudeotides in and around the three-way junction element. These nudeotides help to define the purine-binding pocket through the formation of two Structure of a natural guanine- responsive riboswitch complexed with the metabolite hypoxanthine ets f hakenredly ahove and bealrse UFie-hs2 ha 3a sde of thd a. A23cils.cC3 tiwle n oh cars, the Wiran, ckick face ofthe pocket is flanked by a water-mediated U22-A52-A73 base triple and (Fig. 2a). The other side is created by sequential base triples between conserved Watson-Crick pairs at the top of helix P1 (U20-A76 and Robert T. Batey, Sunny D. Gilbert & Rebecca K. Montange A21-U75)and the Watson-Crick faces of U49 and C50,respectively, Department of Chemistry and Biochemistryy 215 UCB, University of Colorada Boulder, Colorado 80309, USA which fasten the J2/3 loop to the P1 helix. This extensive use of base d-binding site is very similar to Riboswitches are genetic regulatory elements found in the 5' selected RNA aptamers that recognize planar ring systems, as untranslated region of messenger RNA that act in the absence of exemplified by the structures of the theophylie, FMNI0 and protein cofactors1a. They are broadly distributed across bacteria malachite green" binders. Thus, artificially selected RNAs use and account for the regulation of more than 2% of all genes in Bacillus subtilis, underscoring their importance in the control of molecule ligands as their naturally occurring counterpart. some of the same principles for creating binding sites for small- 2004 Nature Publishing GroupExplanation / Answer
1.Riboswitches are genetic regulatory elements found in the 5' untranslated messenger RNA that act in the absence of protein cofactors
2. They are broadly distributed across bacteria account for the regulation of more than 2 percent of all genes of bacillus subtitlis underscoring their importance in the control of cellular metabolism
3.The 5' untranslated region of many MRNAs of genes involved in purine metabolism and transportation chain contain guanine and responsive riboswitch that directly binds guanine, hypoxanthin and xanthine to terminate transcription
4.here we report the crystal structure 1.95Aungstrng resolution of the purine binding domain the guanine riboswitch xpt-pbuX operon of b.subtitils bound to the hypoxanthin ,a prevalent metabolite in bacteria purine salvage pathway
5.The structure reveals the complex RNA fold involving several phylogentically conserved nucleotides that create binding pocket that almost completely envelopes the ligand
6.hypoxanthine functions to stabilize this structure and to promote the formation of a down stream transcriptional terminator element ,there by providing mechanism directly repressing gene expression in response to an intracellular concentrations of metabolite.
Related Questions
Navigate
Integrity-first tutoring: explanations and feedback only — we do not complete graded work. Learn more.