Mapping L1 ligase ribozyme conformational switch. [PDF]
L1 ligase (L1L) molecular switch is an in vitro optimized synthetic allosteric ribozyme that catalyzes the regioselective formation of a 5'-to-3' phosphodiester bond, a reaction for which there is no known naturally occurring RNA catalyst. L1L serves as a proof of principle that RNA can catalyze a critical reaction for prebiotic RNA self-replication ...
Giambaşu GM, Lee TS, Scott WG, York DM.
europepmc +8 more sources
Evolution of the substrate specificity of an RNA ligase ribozyme from phosphorimidazole to triphosphate activation. [PDF]
ABSTRACTThe acquisition of new RNA functions through evolutionary processes would have been essential for the diversification of RNA-based primordial biology and its subsequent transition to modern biology. However, the mechanisms by which RNAs access new functions remain unclear.
DasGupta S +3 more
europepmc +7 more sources
Rational optimization of the DSL ligase ribozyme with GNRA/receptor interacting modules. [PDF]
The DSL ribozyme is a class of artificial ligase ribozymes with a highly modular architecture, which catalyzes template-directed RNA ligation on a helical substrate module that can be either covalently connected (cis-DSL) or physically separated (trans-DSL) from the catalytic module.
Ishikawa J +5 more
europepmc +5 more sources
Systematic minimization of RNA ligase ribozyme through large-scale design-synthesis-sequence cycles. [PDF]
Abstract Template-directed RNA ligation catalyzed by an RNA enzyme (ribozyme) is a plausible and important reaction that could have been involved in transferring genetic information during prebiotic evolution. Laboratory evolution experiments have yielded several classes of ligase ribozymes, but their minimal sequence requirements remain
Nomura Y, Yokobayashi Y.
europepmc +5 more sources
Cross-Catalytic Replication of an RNA Ligase Ribozyme [PDF]
A self-replicating RNA ligase ribozyme was converted to a cross-catalytic format whereby two ribozymes direct each other's synthesis from a total of four component substrates. Each ribozyme binds two RNA substrates and catalyzes their ligation to form the opposing ribozyme.
Dong‐Eun Kim, Gerald F. Joyce
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A complex ligase ribozyme evolved in vitro from a group I ribozyme domain [PDF]
Like most proteins, complex RNA molecules often are modular objects made up of distinct structural and functional domains. The component domains of a protein can associate in alternative combinations to form molecules with different functions. These observations raise the possibility that complex RNAs also can be assembled from preexisting
Luc Jaeger +2 more
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New ligase-derived RNA polymerase ribozymes [PDF]
The search is underway for a catalytic RNA molecule capable of self-replication. Finding such a ribozyme would lend crucial support to the RNA World hypothesis, which holds that very early life-forms relied on RNA for both replicating and storing genetic information.
Michael S. Lawrence, David P. Bartel
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A ligase ribozyme obtained from a structured pool [PDF]
Here we report the in vitro selection experiment employed to construct a catalytic site on a self-folding RNA. To practice the selection, the sequence of 30 nucleotides was located in close proximity of the putative reaction site in a derivative of a naturally occurring RNA with a well known 3D structure.
Wataru Yoshioka
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Application of RtcB ligase to monitor self-cleaving ribozyme activity by RNA-seq [PDF]
Abstract Self-cleaving ribozymes are catalytic RNAs and can be found in all domains of life. They catalyze a site-specific cleavage that results in a 5′ fragment with a 2′,3′ cyclic phosphate (2′,3′ cP) and a 3′ fragment with a 5′ hydroxyl (5′ OH) end. Recently, several strategies to enrich self-cleaving ribozymes by targeted biochemical
V Janett Olzog +4 more
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The three-dimensional architecture of the class I ligase ribozyme [PDF]
The class I ligase ribozyme catalyzes a Mg ++ -dependent RNA-ligation reaction that is chemically analogous to a single step of RNA polymerization. Indeed, this ribozyme constitutes the catalytic domain of an accurate and general RNA polymerase ribozyme.
Nicholas H. Bergman +4 more
openalex +4 more sources

