אסיף מאגר המחקר החקלאי

Sequence-specific recognition of RNA hairpins by the SAM domain of Vts1p

Year:

2006

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Volume :

13

Co-Authors:

Aviv, T., Program in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, 600 University Ave., Toronto, Ont. M5G 1X5, Canada, Department of Molecular and Medical Genetics, University of Toronto, Toronto, Ont. M5S 1A8, Canada
Lin, Z., Program in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, 600 University Ave., Toronto, Ont. M5G 1X5, Canada
Ben-Ari, G., Program in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, 600 University Ave., Toronto, Ont. M5G 1X5, Canada
Smibert, C.A., Department of Biochemistry, University of Toronto, Toronto, Ont. M5S 1A8, Canada
Sicheri, F., Program in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, 600 University Ave., Toronto, Ont. M5G 1X5, Canada, Department of Molecular and Medical Genetics, University of Toronto, Toronto, Ont. M5S 1A8, Canada

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Abstract:

The SAM domain of the Saccharomyces cerevisiae post-transcriptional regulator Vts1p epitomizes a subfamily of SAM domains conserved from yeast to humans that function as sequence-specific RNA-binding domains. Here we report the 2.0-Å X-ray structure of the Vts1p SAM domain bound to a high-affinity RNA ligand. Specificity of RNA binding arises from the association of a guanosine loop base with a shallow pocket on the SAM domain and from multiple SAM domain contacts to the unique backbone structure of the loop, defined in part by a nonplanar base pair within the loop. We have validated NNF1 as an endogenous target of Vts1p among 79 transcripts that copurify with Vts1p. Bioinformatic analysis of these mRNAs demonstrates that the RNA-binding specificity of Vts1p in vivo is probably more stringent than that of the isolated SAM domain in vitro. © 2006 Nature Publishing Group.

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