TY - JOUR
T1 - A specific monovalent metal ion integral to the AA platform of the RNA tetraloop receptor
AU - Basu, Soumitra
AU - Rambo, Robert P.
AU - Strauss-Soukup, Juliane
AU - Cate, Jamie H.
AU - Ferré-D'Amaré, Adrian R.
AU - Strobel, Scott A.
AU - Doudna, Jennifer A.
N1 - Funding Information:
Awards and the Searle Foundation. J.A.D. is a Lucille P. Markey Scholar and a David and Lucile Packard Foundation Fellow. This work was funded by an NSF CAREER award and a JFRA from the ACS to S.A.S., and by an NIH grant to J.A.D.
Funding Information:
We wish to thank P. B. Moore and J. R. Williamson for critical comments on the manuscript. R.P.R. and J.H.C. were supported by the NIH and A.R.F is a Fellow of the Jane Coffin Childs Memorial Fund for Medical Research. J. S.-S. is a Fellow of the NIH. S.A.S. and J.A.D. are both supported by Beckman Young Investigator
Copyright:
Copyright 2007 Elsevier B.V., All rights reserved.
PY - 1998/11
Y1 - 1998/11
N2 - Metal ions are essential for the folding and activity of large catalytic RNAs. While divalent metal ions have been directly implicated in RNA tertiary structure formation, the role of monovalent ions has been largely unexplored. Here we report the first specific monovalent metal ion binding site within a catalytic RNA. As seen crystallographically, a potassium ion is coordinated immediately below AA platforms of the Tetrahymena ribozyme P4-P6 domain, including that within the tetraloop receptor. Interference and kinetic experiments demonstrate that potassium ion binding within the tetraloop receptor stabilizes the folding of the P4-P6 domain and enhances the activity of the Azoarcus group I intron. Since a monovalent ion binding site is integral to the tetraloop receptor, a tertiary structural motif that occurs frequently in RNA, monovalent metal ions are likely to participate in the folding and activity of a wide diversity of RNAs.
AB - Metal ions are essential for the folding and activity of large catalytic RNAs. While divalent metal ions have been directly implicated in RNA tertiary structure formation, the role of monovalent ions has been largely unexplored. Here we report the first specific monovalent metal ion binding site within a catalytic RNA. As seen crystallographically, a potassium ion is coordinated immediately below AA platforms of the Tetrahymena ribozyme P4-P6 domain, including that within the tetraloop receptor. Interference and kinetic experiments demonstrate that potassium ion binding within the tetraloop receptor stabilizes the folding of the P4-P6 domain and enhances the activity of the Azoarcus group I intron. Since a monovalent ion binding site is integral to the tetraloop receptor, a tertiary structural motif that occurs frequently in RNA, monovalent metal ions are likely to participate in the folding and activity of a wide diversity of RNAs.
UR - http://www.scopus.com/inward/record.url?scp=0031790171&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0031790171&partnerID=8YFLogxK
U2 - 10.1038/2960
DO - 10.1038/2960
M3 - Article
C2 - 9808044
AN - SCOPUS:0031790171
VL - 5
SP - 986
EP - 992
JO - Nature Structural and Molecular Biology
JF - Nature Structural and Molecular Biology
SN - 1545-9993
IS - 11
ER -