Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 986-992 |
| Number of pages | 7 |
| Journal | Nature Structural Biology |
| Volume | 5 |
| Issue number | 11 |
| DOIs | |
| State | Published - Nov 1998 |
| Externally published | Yes |
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All Science Journal Classification (ASJC) codes
- Biochemistry
- Structural Biology
- Genetics
Cite this
A specific monovalent metal ion integral to the AA platform of the RNA tetraloop receptor. / Basu, Soumitra; Rambo, Robert P.; Strauss-Soukup, Juliane K.; Cate, Jamie H.; Ferré-D'Amaré, Adrian R.; Strobel, Scott A.; Doudna, Jennifer A.
In: Nature Structural Biology, Vol. 5, No. 11, 11.1998, p. 986-992.Research output: Contribution to journal › Article
}
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 K.
AU - Cate, Jamie H.
AU - Ferré-D'Amaré, Adrian R.
AU - Strobel, Scott A.
AU - Doudna, Jennifer A.
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.
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U2 - 10.1038/2960
DO - 10.1038/2960
M3 - Article
VL - 5
SP - 986
EP - 992
JO - Nature Structural and Molecular Biology
JF - Nature Structural and Molecular Biology
SN - 1545-9993
IS - 11
ER -