[NMR paper] Contribution of protein phosphorylation to binding-induced folding of the SLBP-histone mRNA complex probed by phosphorus-31 NMR.
Contribution of protein phosphorylation to binding-induced folding of the SLBP-histone mRNA complex probed by phosphorus-31 NMR.
Contribution of protein phosphorylation to binding-induced folding of the SLBP-histone mRNA complex probed by phosphorus-31 NMR.
FEBS Open Bio. 2014;4:853-7
Authors: Thapar R
Abstract
Phosphorus-31 ((31)P) NMR can be used to characterize the structure and dynamics of phosphorylated proteins. Here, I use (31)P NMR to report on the chemical nature of a phosphothreonine that lies in the RNA binding domain...
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11-08-2014 12:43 PM
Contribution of protein phosphorylation to binding-induced folding of the SLBP–histone mRNA complex probed by phosphorus-31 NMR
Contribution of protein phosphorylation to binding-induced folding of the SLBP–histone mRNA complex probed by phosphorus-31 NMR
Publication date: Available online 16 October 2014
Source:FEBS Open Bio</br>
Author(s): Roopa Thapar</br>
Phosphorus-31 (31P) NMR can be used to characterize the structure and dynamics of phosphorylated proteins. Here, I use 31P NMR to report on the chemical nature of a phosphothreonine that lies in the RNA binding domain of SLBP (stem-loop binding protein). SLBP is an intrinsically disordered protein and phosphorylation at this threonine...
Modular protein-RNA interactions regulating mRNA metabolism: a role for NMR.
Modular protein-RNA interactions regulating mRNA metabolism: a role for NMR.
Modular protein-RNA interactions regulating mRNA metabolism: a role for NMR.
Eur Biophys J. 2011 Apr 7;
Authors: Cukier CD, Ramos A
Here we review the role played by transient interactions between multi-functional proteins and their RNA targets in the regulation of mRNA metabolism, and we describe the important function of NMR spectroscopy in the study of these systems. We place emphasis on a general approach for the study of different features of modular multi-domain...
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NMR structure of the let-7 miRNA interacting with the site LCS1 of lin-41 mRNA from Caenorhabditis elegans.
NMR structure of the let-7 miRNA interacting with the site LCS1 of lin-41 mRNA from Caenorhabditis elegans.
NMR structure of the let-7 miRNA interacting with the site LCS1 of lin-41 mRNA from Caenorhabditis elegans.
Nucleic Acids Res. 2010 Nov 1;38(21):7814-21
Authors: Cevec M, Thibaudeau C, Plavec J
We have determined the 3D structure of a 34-nt RNA construct, herein named LCS1co, which mimics the interaction of let-7 microRNA (miRNA) to one of its complementary binding sites, LCS1, in the 3'-untranslated region of lin-41 mRNA by solution-state...
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01-14-2011 12:05 PM
[NMR paper] Joint X-ray and NMR refinement of the yeast L30e-mRNA complex.
Joint X-ray and NMR refinement of the yeast L30e-mRNA complex.
Related Articles Joint X-ray and NMR refinement of the yeast L30e-mRNA complex.
Structure. 2004 Jul;12(7):1165-76
Authors: Chao JA, Williamson JR
L30e, a Saccharomyces cervisiae ribosomal protein, regulates its own expression by binding to a purine-rich asymmetric internal loop located in both its pre-mRNA and mature mRNA. A crystal structure of an MBP-L30e fusion protein in complex with an RNA containing the pre-mRNA regulatory site was solved at 3.24 A. Interestingly, the...
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11-24-2010 09:51 PM
[NMR paper] NMR structure and dynamics of the RNA-binding site for the histone mRNA stem-loop bin
NMR structure and dynamics of the RNA-binding site for the histone mRNA stem-loop binding protein.
Related Articles NMR structure and dynamics of the RNA-binding site for the histone mRNA stem-loop binding protein.
RNA. 2002 Jan;8(1):83-96
Authors: DeJong ES, Marzluff WF, Nikonowicz EP
The 3' end of replication-dependent histone mRNAs terminate in a conserved sequence containing a stem-loop. This 26-nt sequence is the binding site for a protein, stem-loop binding protein (SLBP), that is involved in multiple aspects of histone mRNA metabolism...
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11-24-2010 08:49 PM
[NMR paper] 1H-NMR studies on association of mRNA cap-analogues with tryptophan-containing peptid
1H-NMR studies on association of mRNA cap-analogues with tryptophan-containing peptides.
Related Articles 1H-NMR studies on association of mRNA cap-analogues with tryptophan-containing peptides.
Biochim Biophys Acta. 1996 Mar 7;1293(1):97-105
Authors: Stolarski R, Sitek A, StepiÅ?ski J, Jankowska M, Oksman P, Temeriusz A, Darzynkiewicz E, Lönnberg H, Shugar D
1H-NMR spectroscopy was applied to a study of the mode of interaction, in aqueous medium in the pH range 5.2-8.5 and at low and high temperatures, between several mono- and dinucleotide...