Use of Phosphorothioates to Identify Sites of Metal-Ion Binding in RNA

scientific article published on November 17, 2009

Use of Phosphorothioates to Identify Sites of Metal-Ion Binding in RNA is …
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scholarly articleQ13442814

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P356DOI10.1016/S0076-6879(09)68015-0
P698PubMed publication ID20946776

P50authorDaniel HerschlagQ5217478
P2093author name stringMarcello Forconi
P2860cites workFunctional identification of catalytic metal ion binding sites within RNA.Q24812515
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Crystal structure of a phage Twort group I ribozyme-product complexQ28296661
Three metal ions at the active site of the Tetrahymena group I ribozymeQ28315032
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Catalysis of RNA cleavage by the Tetrahymena thermophila ribozyme. 1. Kinetic description of the reaction of an RNA substrate complementary to the active siteQ30455689
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A second catalytic metal ion in group I ribozymeQ30470964
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Stereochemical course of catalysis by the Tetrahymena ribozymeQ34413657
Structural evidence for a two-metal-ion mechanism of group I intron splicingQ34448249
Evidence that binding of C5 protein to P RNA enhances ribozyme catalysis by influencing active site metal ion affinityQ35946148
Stability constants of magnesium and cadmium complexes of adenine nucleotides and thionucleotides and rate constants for formation and dissociation of magnesium-ATP and magnesium-ADPQ36599356
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The role of the cleavage site 2'-hydroxyl in the Tetrahymena group I ribozyme reactionQ38315719
Probing the role of metal ions in RNA catalysis: kinetic and thermodynamic characterization of a metal ion interaction with the 2'-moiety of the guanosine nucleophile in the Tetrahymena group I ribozymeQ38321270
Evidence for a polynuclear metal ion binding site in the catalytic domain of ribonuclease P RNA.Q39647190
Metal ion interaction with cosubstrate in self-splicing of group I intronsQ39719033
Distinct sites of phosphorothioate substitution interfere with folding and splicing of the Anabaena group I intronQ40848247
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Functional identification of ligands for a catalytic metal ion in group I intronsQ41838616
Identification of phosphates involved in catalysis by the ribozyme RNase P RNAQ42101917
Identification by modification-interference of purine N-7 and ribose 2'-OH groups critical for catalysis by bacterial ribonuclease P.Q43206276
Site-specific modification of pre-mRNA: the 2'-hydroxyl groups at the splice sitesQ43506774
The tetrahymena ribozyme cleaves a 5'-methylene phosphonate monoester approximately 10(2)-fold faster than a normal phosphate diester: implications for enzyme catalysis of phosphoryl transfer reactionsQ43733367
Geometric characteristics of hydrogen bonds involving sulfur atoms in proteinsQ46194094
Chain length determination of small double- and single-stranded DNA molecules by polyacrylamide gel electrophoresisQ50850873
Metal coordination sites that contribute to structure and catalysis in the group I intron from TetrahymenaQ52225074
Hard and Soft Acids and BasesQ55872041
Absolute hardness: companion parameter to absolute electronegativityQ55887290
Directionality of Hydrogen Bonds to Sulfur and OxygenQ58486760
A chemical phylogeny of group I introns based upon interference mapping of a bacterial ribozymeQ74259009
A new metal ion interaction in the Tetrahymena ribozyme reaction revealed by double sulfur substitutionQ77318709
P407language of work or nameEnglishQ1860
P304page(s)311-333
P577publication date2009-11-17
P1433published inMethods in EnzymologyQ2076903
P1476titleUse of Phosphorothioates to Identify Sites of Metal-Ion Binding in RNA
P478volume468

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cites work (P2860)
Q36766768A targeted DNA substrate mechanism for the inhibition of HIV-1 integrase by inhibitors with antiretroviral activity
Q24617627Biological phosphoryl-transfer reactions: understanding mechanism and catalysis
Q35682190Ground-state coordination of a catalytic metal to the scissile phosphate of a tertiary-stabilized Hammerhead ribozyme
Q42155694Metal-ion rescue revisited: biochemical detection of site-bound metal ions important for RNA folding
Q36586267Nuclease-Resistant c-di-AMP Derivatives That Differentially Recognize RNA and Protein Receptors

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