## Abstract The bacterial __glmS__ ribozyme is mechanistically unique among both riboswitches and RNA catalysts. Its selfβcleavage activity is the basis of riboswitch regulation of glucosamineβ6βphosphate (GlcN6P) production, and catalysis requires GlcN6P as a coenzyme. Previous work has shown that
Self-Incorporation of coenzymes by ribozymes
β Scribed by Ronald R. Breaker; Gerald F. Joyce
- Book ID
- 104649163
- Publisher
- Springer
- Year
- 1995
- Tongue
- English
- Weight
- 876 KB
- Volume
- 40
- Category
- Article
- ISSN
- 0022-2844
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β¦ Synopsis
RNA molecules that are assembled from the four standard nucleotides contain a limited number of chemical functional groups, a characteristic that is generally thought to restrict the potential for catalysis by ribozymes. Although polypeptides carry a wider range of functional groups, many contemporary protein-based enzymes employ coenzymes to augment their capabilities. The coenzymes possess additional chemical moieties that can participate directly in catalysis and thereby enhance catalytic function. In this work, we demonstrate a mechanism by which ribozymes can supplement their limited repertoire of functional groups through RNAcatalyzed incorporation of various coenzymes and coenzyme analogues. The group I ribozyme of Tetrahymena thermophila normally mediates a phosphoester transfer reaction that results in the covalent attachment of guanosine to the ribozyme. Here, a shortened version of the ribozyme is shown to catalyze the self-incorporation of coenzymes and coenzyme analogues, such as NAD Γ· and dephosphorylated CoA-SH. Similar ribozyme activities may have played an important role in the "RNA world," when RNA enzymes are thought to have maintained a complex metabolism in the absence of proteins and would have benefited from the inclusion of additional functional groups.
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