Related ArticlesInteractions of a didomain fragment of the Drosophila sex-lethal protein with single-stranded uridine-rich oligoribonucleotides derived from the transformer and Sex-lethal messenger RNA precursors: NMR with residue-selective [5-2H]uridine substitutions.
J Biomol NMR. 2000 Jun;17(2):153-65
Authors: Kim I, Muto Y, Watanabe S, Kitamura A, Futamura Y, Yokoyama S, Hosono K, Kawai G, Takaku H, Dohmae N, Takio K, Saskamoto H, Shimura Y
Proteins that contain two or more copies of the RNA-binding domain [ribonucleoprotein (RNP) domain or RNA recognition motif (RRM)] are considered to be involved in the recognition of single-stranded RNA, but the mechanisms of this recognition are poorly understood at the molecular level. For an NMR analysis of a single-stranded RNA complexed with a multi-RBD protein, residue-selective stable-isotope labeling techniques are necessary, rather than common assignment methods based on the secondary structure of RNA. In the present study, we analyzed the interaction of a Drosophila Sex-lethal (Sx1) protein fragment, consisting of two RBDs (RBD1-RBD2), with two distinct target RNAs derived from the tra and Sxl mRNA precursors with guanosine and adenosine, respectively, in a position near the 5'-terminus of a uridine stretch. First, we prepared a [5-2H]uridine phosphoramidite, and synthesized a series of 2H-labeled RNAs, in which all of the uridine residues except one were replaced by [5-2H]uridine in the target sequence, GU8C. By observing the H5-H6 TOCSY cross peaks of the series of 2H-labeled RNAs complexed with the Sx1 RBDI-RBD2, all of the base H5-H6 proton resonances of the target RNA were unambiguously assigned. Then, the H5-H6 cross peaks of other target RNAs, GU2GU8, AU8, and UAU8, were assigned by comparison with those of GU8C. We found that the uridine residue prior to the G or A residue is essential for proper interaction with the protein, and that the interaction is tighter for A than for G. Moreover, the H1' resonance assignments were achieved from the H5-H6 assignments. The results revealed that all of the protein-bound nucleotide residues, except for only two, are in the unusual C2'-endo ribose conformation in the complex.
NMR studies of the solution conformation of the sex peptide from Drosophila melanogaster.
NMR studies of the solution conformation of the sex peptide from Drosophila melanogaster.
NMR studies of the solution conformation of the sex peptide from Drosophila melanogaster.
FEBS Lett. 2011 Apr 20;585(8):1197-202
Authors: Moehle K, Freund A, Kubli E, Robinson JA
The insect sex peptide (SP) elicits a variety of biological responses upon transfer to the mated female. SP contains 36 amino acids, including a tryptophan-rich N-terminal region, a central region containing five hydroxyproline (Hyp) residues, and a C-terminal region enclosed by a...
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Target immobilization as a strategy for NMR-based fragment screening: comparison of TINS, STD, and SPR for fragment hit identification.
Target immobilization as a strategy for NMR-based fragment screening: comparison of TINS, STD, and SPR for fragment hit identification.
Target immobilization as a strategy for NMR-based fragment screening: comparison of TINS, STD, and SPR for fragment hit identification.
J Biomol Screen. 2010 Sep;15(8):978-89
Authors: Kobayashi M, Retra K, Figaroa F, Hollander JG, Ab E, Heetebrij RJ, Irth H, Siegal G
Fragment-based drug discovery (FBDD) has become a widely accepted tool that is complementary to high-throughput screening (HTS) in developing...
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01-13-2011 12:00 PM
[NMR paper] NMR and ICP spectroscopic analysis of the DNA-binding domain of the Drosophila GCM pr
NMR and ICP spectroscopic analysis of the DNA-binding domain of the Drosophila GCM protein reveals a novel Zn2+ -binding motif.
Related Articles NMR and ICP spectroscopic analysis of the DNA-binding domain of the Drosophila GCM protein reveals a novel Zn2+ -binding motif.
Protein Eng. 2003 Apr;16(4):247-54
Authors: Shimizu M, Hiroaki H, Kohda D, Hosoya T, Akiyama-Oda Y, Hotta Y, Morita EH, Morikawa K
Drosophila GCM (glial cell missing) is a novel DNA-binding protein that determines the fate of glial precursors from the neural default to glia....
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[NMR paper] Interactions of a vesicular stomatitis virus G protein fragment with phosphatidylseri
Interactions of a vesicular stomatitis virus G protein fragment with phosphatidylserine: NMR and fluorescence studies.
Related Articles Interactions of a vesicular stomatitis virus G protein fragment with phosphatidylserine: NMR and fluorescence studies.
Biochim Biophys Acta. 1998 Dec 9;1415(1):101-13
Authors: Hall MP, Burson KK, Huestis WH
The interaction of a 19 amino acid vesicular stomatitis virus G protein fragment (GTWLNPGFPPQSCGYATVT) with phosphatidylserine-containing model membranes was investigated using solution-phase 1d and 2d 1H...
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[NMR paper] NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reve
NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5.
EMBO J. 1995 Jul 17;14(14):3563-71
Authors: Bycroft M, Grünert S, Murzin AG, Proctor M, St Johnston D
The...
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[NMR paper] Structural and dynamic properties of the Fv fragment and the single-chain Fv fragment
Structural and dynamic properties of the Fv fragment and the single-chain Fv fragment of an antibody in solution investigated by heteronuclear three-dimensional NMR spectroscopy.
Related Articles Structural and dynamic properties of the Fv fragment and the single-chain Fv fragment of an antibody in solution investigated by heteronuclear three-dimensional NMR spectroscopy.
Biochemistry. 1994 Mar 22;33(11):3296-303
Authors: Freund C, Ross A, Plückthun A, Holak TA
Fv fragments, heterodimers of the variable light (VL) and variable heavy chain...
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[NMR paper] Structural and dynamic properties of the Fv fragment and the single-chain Fv fragment
Structural and dynamic properties of the Fv fragment and the single-chain Fv fragment of an antibody in solution investigated by heteronuclear three-dimensional NMR spectroscopy.
Related Articles Structural and dynamic properties of the Fv fragment and the single-chain Fv fragment of an antibody in solution investigated by heteronuclear three-dimensional NMR spectroscopy.
Biochemistry. 1994 Mar 22;33(11):3296-303
Authors: Freund C, Ross A, Plückthun A, Holak TA
Fv fragments, heterodimers of the variable light (VL) and variable heavy chain...