NDLI: A comparison of two classic Pb<sup>2+</sup>-dependent RNA-cleaving DNAzymes

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Two-dimensional layered nanomaterials for gas-sensing applications

Intercalation in two-dimensional transition metal chalcogenides

A new sodium storage mechanism of TiO₂ for sodium ion batteries

Coupling of terminal iridium nitrido complexes

Alkoxide-intercalated NiFe-layered double hydroxides magnetic nanosheets as efficient water oxidation electrocatalysts

Cu₂O clusters grown on TiO₂ nanoplates as efficient photocatalysts for hydrogen generation

A comparison of two classic Pb²⁺-dependent RNA-cleaving DNAzymes

Sustainable development of a surface-functionalized mesoporous aluminosilicate with ultra-high ion exchange efficiency

Glutathione modified carbon-dots: from aggregation-induced emission enhancement properties to a “turn-on” sensing of temperature/Fe³⁺ ions in cells

Thioether-terminated nickel(ii) coordination clusters with {Ni₆} horseshoe- and {Ni₈} rollercoaster-shaped cores

MoS₂ with an intercalation reaction as a long-life anode material for lithium ion batteries

Dioxygen binding at a four-coordinate cobaltous porphyrin site in a metal–organic framework: structural, EPR, and O₂ adsorption analysis

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Carbamide promoted polyol synthesis and transmittance properties of silver nanocubes

Correction: Alkoxide-intercalated NiFe-layered double hydroxides magnetic nanosheets as efficient water oxidation electrocatalysts

Correction: A new methylviologen-templated zinc gallophosphate zeolite with photo-/thermochromism, fluorescent and photoelectric properties

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A comparison of two classic Pb²⁺-dependent RNA-cleaving DNAzymes

Content Provider	Royal Society of Chemistry (RSC)
Author	Saran, Runjhun Liu, Juewen
Copyright Year	2016
Abstract	Pb2+ is a very important metal cofactor in DNAzyme catalysis. GR5 is the first reported DNAzyme, and 17E is the most thoroughly studied. Both have the highest activity with Pb2+ and are by far the fastest RNA-cleaving DNAzymes. GR5 reacts only with Pb2+ while 17E is also active with a number of other divalent metal ions. It is also interesting to note that Pb2+ shows activity with most RNA-cleaving DNAzymes. To understand these Pb2+-dependent DNAzymes and the occurrence of DNAzyme sequences, herein systematic mutation studies are performed on GR5. A comparison with 17E is also made. The A6, G7, C13, and G14 positions in 17E have been previously established to be crucial and we report A6, G7, C14, and G15 in GR5 to have the same role. The guanine at the cleavage site dinucleotide junction of the substrate strand is also mutated to hypoxanthine, 2-aminopurine, and adenine. Again, both enzymes show the same trend of activity change. Our results suggest that both DNAzymes have a similar binding pocket for Pb2+. The reason for Pb2+ being active in many DNAzymes is attributed to its simple binding motif requirement. Finally, we propose that 17E is a special form of GR5. They both have the simple sequence requirements needed for Pb2+-dependent activity, but 17E has additional motifs making it active also with other divalent metal ions.
Starting Page	494
Ending Page	501
Page Count	8
File Format	HTM / HTML PDF
ISSN	20521553
Volume Number	3
Issue Number	4
Journal	Inorganic Chemistry Frontiers
DOI	10.1039/c5qi00125k
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Cofactor (biochemistry) GR 5 Mutation Group of Eight Group of 15 Guanine Hypoxanthine 2-Aminopurine Adenine
Content Type	Text
Resource Type	Article
Subject	Inorganic Chemistry

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A comparison of two classic Pb2+-dependent RNA-cleaving DNAzymes

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