Metal ion-promoted cleavage of mRNA 5′-cap models: hydrolysis of the triphosphate bridge and reactions of the N7-methylguanine base

Valakoski, Satu; Heiskanen, Suvi; Andersson, Sanna; Lähde, Mari; Mikkola, Satu

doi:10.1039/b108222a

Cited by 16 publications

(35 citation statements)

References 39 publications

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“…There are a few other examples in the literature when the formation of different by-products during the hydrolytic cleavage of cap-analogues have been reported [26,29,32,34]. In one of these studies, the copper(II)-TerPy complex enhanced the hydrolysis of ApppA and according to the HPLC-MS/MS analysis of reaction samples, a HEPES-AMP adduct was formed as a byproduct [26].…”

Section: Kinetic Studies In the Zinc(ii)-tmci Systemmentioning

confidence: 95%

“…In one of these studies, the copper(II)-TerPy complex enhanced the hydrolysis of ApppA and according to the HPLC-MS/MS analysis of reaction samples, a HEPES-AMP adduct was formed as a byproduct [26]. The possibility of the existence of similar by-products in the present system have been excluded by performing the reaction in the absence of MOBS buffer and omitting EDTA from the eluent used for the HPLC analysis.…”

Section: Kinetic Studies In the Zinc(ii)-tmci Systemmentioning

confidence: 97%

“…According to the reported activities, the Lewis-acidity of the metal ions plays a rather important but certainly not exclusive role in promoting the process. Examples of efficient cleavage by complexes of copper(II) and trivalent lanthanide ions have been reported [26][27][28][29][30][31][32], whereas the catalysis by monomeric zinc(II) complexes is modest [26][27][28]31]. The rate of the cleavage was found to be second-order on the concentration of simple copper(II) complexes [26].…”

Section: Introductionmentioning

confidence: 93%

“…Similarly to the internucleosidic phosphodiester bonds of RNA or RNA model substrates, the hydrolysis of the triphosphate bridge in cap-models can also be enhanced by metal ions and their complexes [24][25][26][27][28][29][30][31][32]. According to the reported activities, the Lewis-acidity of the metal ions plays a rather important but certainly not exclusive role in promoting the process.…”

Section: Introductionmentioning

confidence: 98%

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Hydrolysis of a mRNA 5′-cap model substrate, 5′,5′-ApppA by di- and trinuclear zinc(II) complexes of a polyamino-polyol ligand

Jancsó

Mikkola

Lönnberg

et al. 2005

Journal of Inorganic Biochemistry

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Section: Kinetic Studies In the Zinc(ii)-tmci Systemmentioning

confidence: 95%

Section: Kinetic Studies In the Zinc(ii)-tmci Systemmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 93%

Section: Introductionmentioning

confidence: 98%

See 2 more Smart Citations

Hydrolysis of a mRNA 5′-cap model substrate, 5′,5′-ApppA by di- and trinuclear zinc(II) complexes of a polyamino-polyol ligand

Jancsó

Mikkola

Lönnberg

et al. 2005

Journal of Inorganic Biochemistry

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“…In a sequence of processes, the base is cleaved, and eventually the N-glycosidic bond is broken [20]. We have previously attempted to enhance this reaction by organic and inorganic nucleophiles under neutral conditions, but only very modest rate enhancements have been achieved [18]. In the present work, we extend the studies to macrocyclic polyamine ligands, substituted with a 2-hydroxyethyl or 2-aminoethyl side arm, to study whether the catalytic activity of metal ion complexes or ligands alone could be enhanced by the presence of an additional amine or hydroxy nucleophile.…”

mentioning

confidence: 98%

Metal Ion Complexes of Macrocyclic Polyamines Enhance Both the Phosphate Hydrolysis and Imidazole Ring Opening of RNA 5′-capStructure

Zhang

Lönnberg

Mikkola

2005

Chemistry & Biodiversity

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The cleavage of P1-(7-methylguanosyl-5') P3-(guanosyl-5') triphosphate, a RNA 5'-cap model, by 2-hydroxyethyl- (6a-6c) and 2-aminoethyl- (7a-7c) substituted macrocycles in the presence and absence of Zn2+ and Cu2+ ions has been studied at pH 7.2 and 60 degrees. In the presence of the metal ions, hydrolysis of the phosphate group is enhanced. The mono- and dinuclear Zn2+ complexes promote solely the phosphate hydrolysis, whereas the corresponding Cu2+ complexes accelerate both the phosphate hydrolysis and the imidazole ring opening of the 7-methylguanine base. In the absence of the metal ions, the macrocycles mainly promote breakdown of the 7-methylguanine base, most probably by enhancing the nucleophilic attack of hydroxide ion on the C(8)-atom by shielding the repulsive negative charge on the phosphate moiety. The 2-hydroxyethyl and 2-aminoethyl side arms exhibit a two- to three-fold rate acceleration. Opening of the imidazole ring eventually results in cleavage of the triphosphate bridge.

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Influence of naturally‐occurring 5′‐pyrophosphate‐linked substituents on the binding of adenylic inhibitors to ribonuclease a: An X‐ray crystallographic study

et al. 2009

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Ribonuclease A is the archetype of a functionally diverse superfamily of vertebrate-specific ribonucleases. Inhibitors of its action have potential use in the elucidation of the in vivo roles of these enzymes and in the treatment of pathologies associated therewith. Derivatives of adenosine 5′-pyrophosphate are the most potent nucleotide-based inhibitors known. Here, we use X-ray crystallography to visualize the binding of four naturally-occurring derivatives that contain 5′-pyrophosphate-linked extensions. 5′-ATP binds with the adenine occupying the B2 subsite in the manner of an RNA substrate but with the γ-phosphate at the P1 subsite. Diadenosine triphosphate (Ap3A) binds with the adenine in syn conformation, the β-phosphate as the principal P1 subsite ligand and without order beyond the γ-phosphate. NADPH and NADP+ bind with the adenine stacked against an alternative rotamer of His119, the 2′-phosphate at the P1 subsite, and without order beyond the 5′-α-phosphate. We also present the structure of the complex formed with pyrophosphate ion. The structural data enable existing kinetic data on the binding of these compounds to a variety of ribonucleases to be rationalized and suggest that as the complexity of the 5′-linked extension increases, the need to avoid unfavorable contacts places limitations on the number of possible binding modes. © 2009 Wiley Periodicals, Inc. Biopolymers 91: 995–1008, 2009.This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

show abstract

Metal ion-promoted cleavage of mRNA 5′-cap models: hydrolysis of the triphosphate bridge and reactions of the N7-methylguanine base

Cited by 16 publications

References 39 publications

Hydrolysis of a mRNA 5′-cap model substrate, 5′,5′-ApppA by di- and trinuclear zinc(II) complexes of a polyamino-polyol ligand

Hydrolysis of a mRNA 5′-cap model substrate, 5′,5′-ApppA by di- and trinuclear zinc(II) complexes of a polyamino-polyol ligand

Metal Ion Complexes of Macrocyclic Polyamines Enhance Both the Phosphate Hydrolysis and Imidazole Ring Opening of RNA 5′-capStructure

Influence of naturally‐occurring 5′‐pyrophosphate‐linked substituents on the binding of adenylic inhibitors to ribonuclease a: An X‐ray crystallographic study

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