נגישות
menu      
Advanced Search
Syntax
Search...
Volcani treasures
About
Terms of use
Manage
Community:
אסיף מאגר המחקר החקלאי
Powered by ClearMash Solutions Ltd -
Sequence-specific recognition of RNA hairpins by the SAM domain of Vts1p
Year:
2006
Authors :
Ben-Ari, Giora
;
.
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
Facilitators :
From page:
168
To page:
176
(
Total pages:
9
)
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.
Note:
Related Files :
bioinformatics
guanosine
Models, Molecular
RNA
Saccharomyces cerevisiae Proteins
unclassified drug
vts1p protein
Show More
Related Content
More details
DOI :
10.1038/nsmb1053
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
29155
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:44
Scientific Publication
Sequence-specific recognition of RNA hairpins by the SAM domain of Vts1p
13
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
Sequence-specific recognition of RNA hairpins by the SAM domain of Vts1p
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.
Scientific Publication
You may also be interested in