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Titolo:
Biochemical detection of monovalent metal ion binding sites within RNA
Autore:
Basu, S; Strobel, SA;
Indirizzi:
Yale Univ, Dept Mol Biophys & Biochem, New Haven, CT 06520 USA Yale Univ New Haven CT USA 06520 ophys & Biochem, New Haven, CT 06520 USA Yale Univ, Dept Chem, New Haven, CT 06520 USA Yale Univ New Haven CT USA 06520 Univ, Dept Chem, New Haven, CT 06520 USA
Titolo Testata:
METHODS
fascicolo: 3, volume: 23, anno: 2001,
pagine: 264 - 275
SICI:
1046-2023(200103)23:3<264:BDOMMI>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
RIBONUCLEASE-P RIBOZYME; GROUP-I INTRON; TETRAHYMENA RIBOZYME; TERTIARY STRUCTURE; CRYSTAL-STRUCTURE; FUNCTIONAL-GROUPS; PYRUVATE-KINASE; CLEAVAGE SITE; P4-P6 DOMAIN; CORE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Strobel, SA Yale Univ, Dept Mol Biophys & Biochem, 260 Whitney Ave,POB 208114, New Haven, CT 06520 USA Yale Univ 260 Whitney Ave,POB 208114 New HavenCT USA 06520 SA
Citazione:
S. Basu e S.A. Strobel, "Biochemical detection of monovalent metal ion binding sites within RNA", METHODS, 23(3), 2001, pp. 264-275

Abstract

Many RNAs, including the ribosome, RNase P, and the group II intron, explicitly require monovalent cations for activity in vitro. Although the necessity of monovalent cations for RNA function has been known for more than a quarter of a century, the characterization of specific monovalent metal sites within large RNAs has been elusive. Here we describe a biochemical approach to identify functionally important monovalent cations in nucleic acids. This method uses thallium (Tl+), a soft Lewis acid heavy metal cation with chemical properties similar to those of the physiological alkaline earth metal potassium (Ki). Nucleotide analog interference mapping (NAIM) with the sulfur-substituted nucleotide 6-thioguanosine in combination with selectivemetal rescue of the interference with Tl+ provides a distinct biochemical signature for monovalent metal ion binding. This approach has identified a K+ binding site within the P4-P6 domain of the Tetrahymena group I intron that is also present within the X-ray crystal structure. The technique also predicted a similar binding site within the Azoarcus group I intron where the structure is not known. The approach is applicable to any RNA molecule that can be transcribed in vitro and whose function can be assayed. (C) 2001Academic Press.

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Documento generato il 04/04/20 alle ore 08:42:25