@article { ISI:000258950500040,
	title = {Changes in dynamics of SRE-RNA on binding to the VTS1p-SAM domain studied by C-13 NMR relaxation},
	journal = {Journal of the American Chemical Society},
	volume = {130},
	number = {36},
	year = {2008},
	month = {SEP},
	pages = {12007-12020},
	publisher = {AMER CHEMICAL SOC},
	type = {Article},
	address = {1155 16TH ST, NW, WASHINGTON, DC 20036 USA},
	abstract = {<p>RNA recognition by proteins is often accompanied by significant changes in RNA dynamics in addition to conformational changes. However, there are very few studies which characterize the changes in molecular motions in RNA on protein binding. We present a quantitative C-13 NMR relaxation study of the changes in RNA dynamics in the pico-nanosecond time scale and micro-millisecond time scale resulting from interaction of the stem-loop SRE-RNA with the VTS1p-SAM domain. C-13 relaxation rates of the protonated carbons of the nucleotide base and anomeric carbons have been analyzed by employing the model-free formalism, for a fully C-13/N-15-labeled sample of the SRE-RNA in the free and protein-bound forms. In the free RNA, the nature of molecular motions are found to be distinctly different in the stem and the loop region. On binding to the protein, the nature of motions becomes more homogeneous throughout the RNA, with many residues showing increased flexibility at the aromatic carbon sites, while the anomeric carbon sites become more rigid. Surprisingly, we also observe indications of a slow collective motion of the RNA in the binding pocket of the protein. The observation of increased motions on binding is interesting in the context of growing evidence that binding does not always lead to motional restrictions and the resulting entropy gain could favor the free energy of association.</p>},
	issn = {0002-7863},
	doi = {10.1021/ja8023115},
	author = {Oberstrass, Florian C. and Allain, Frederic H. T. and Ravindranathan, Sapna}
}
@article { ISI:000275328500024,
	title = {Increase in backbone mobility of the VTS1p-SAM domain on binding to SRE-RNA},
	journal = {Journal of Molecular Biology},
	volume = {396},
	number = {3},
	year = {2010},
	month = {FEB},
	pages = {732-746},
	publisher = {ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD},
	address = {24-28 OVAL RD, LONDON NW1 7DX, ENGLAND},
	abstract = {<p>The sterile alpha motif (SAM) domain of VTS1p, a posttranscriptional gene regulator, belongs to a family of SAM domains conserved from yeast to humans. Even though SAM domains were originally classified as protein-protein interaction domains, recently, it was shown that the yeast VTS1p-SAM and the SAM domain of its Drosophila homolog Smaug can specifically recognize RNA hairpins termed Smaug recognition element (SRE). Structural studies of the SRE-RNA complex of VTS1p-SAM revealed that the SAM domain primarily recognizes the shape of the RNA fold induced by the Watson-Crick base-pairing in the RNA pentaloop. Only the central G nucleotide is specifically recognized. The VTS1p-SAM domain recognizes SRE-RNAs with a CNGGN pentaloop where N is any nucleotide. The C1-G4 base pair in the wild type can be replaced by any pair of nucleotides that can form base pairs even though the binding affinity is greatest with a pyrimidine in position 1 and a purine in position 4. The interaction thus combines elements of sequence-specific and non-sequence-specific recognitions. The lack of structural rearrangements in either partner following binding is rather intriguing, suggesting that molecular dynamics may play an important role in imparting relaxed specificity with respect to the exact combination of nucleotides in the loop, except for the central nucleotide. In this work, we extend our previous studies of SRE-RNA interaction with VTS1p, by comparing the dynamics of the VTS1p-SAM domain both in its free form and when bound to SRE-RNA. The 1 5 N relaxation studies of backbone dynamics suggest the presence of a dynamic interaction interface, with residues associated with specific G3 recognition becoming more rigid on RNA binding while other regions attain increased flexibility. The results parallel the observations from our studies of dynamics changes in SRE-RNA upon binding to VTS1p-SAM and shows that molecular dynamics could play a crucial role in modulating binding affinity and possibly contribute to the free energy of the interaction through an entropy-driven mechanism. (C) 2009 Elsevier Ltd. All rights reserved.</p>},
	keywords = {(15)N relaxation, NMR, protein-RNA interaction, SRE-RNA, VTS1p-SAM domain},
	issn = {0022-2836},
	doi = {10.1016/j.jmb.2009.12.004},
	author = {Ravindranathan, Sapna and Oberstrass, Florian C. and Allain, Frederic H. T.}
}
@article { ISI:000287056000001,
	title = {Structure determination and dynamics of protein-RNA complexes by NMR spectroscopy},
	journal = {Progress in Nuclear Magnetic Resonance Spectroscopy},
	volume = {58},
	number = {1-2},
	year = {2011},
	month = {FEB},
	pages = {1-61},
	publisher = {PERGAMON-ELSEVIER SCIENCE LTD},
	address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND},
	keywords = {Dynamics, NMR spectroscopy, Protein-RNA complex, Structure determination},
	issn = {0079-6565},
	doi = {10.1016/j.pnmrs.2010.10.001},
	author = {Dominguez, Cyril and Schubert, Mario and Duss, Olivier and Ravindranathan, Sapna and Allain, Frederic H. T.}
}
