Hairpin Ribozyme
From Proteopedia
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The hairpin ribozyme is a member of a small family of RNA endonucleases that includes hammerhead, hepatitis delta, and Neurospora VS. Endonucleases are enzymes that cleave phosphodiester bonds within polynucleotide chains. This group of endonucleases cleave RNA substrates in a reversible reaction that generates a 2', 3'-cyclic phosphate and a 5'-hydroxyl termini.<ref>PMID: 10715200</ref> | The hairpin ribozyme is a member of a small family of RNA endonucleases that includes hammerhead, hepatitis delta, and Neurospora VS. Endonucleases are enzymes that cleave phosphodiester bonds within polynucleotide chains. This group of endonucleases cleave RNA substrates in a reversible reaction that generates a 2', 3'-cyclic phosphate and a 5'-hydroxyl termini.<ref>PMID: 10715200</ref> | ||
| - | The hairpin ribozyme was discovered in the negative strand of the tobacco ringspot virus satellite RNA. Study of hairpin ribozyme reaction mechanisms provided early evidence that ribozymes are able to exploit a variety of strategies, just like protein enzymes. But, the hairpin ribozyme has a unique characteristic. Unlike other ribozymes, the hairpin ribozyme does not require metal ions for cleavage or ligation of substrate RNA. | + | The hairpin ribozyme was discovered in the negative strand of the tobacco ringspot virus (TRSV) satellite RNA. Study of hairpin ribozyme reaction mechanisms provided early evidence that ribozymes are able to exploit a variety of strategies, just like protein enzymes. But, the hairpin ribozyme has a unique characteristic. Unlike other ribozymes, the hairpin ribozyme does not require metal ions for cleavage or ligation of substrate RNA. |
<scene name='56/560862/Crystal_structure/1'>catalytically active</scene> | <scene name='56/560862/Crystal_structure/1'>catalytically active</scene> | ||
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==Structure== | ==Structure== | ||
In the transition state, the <scene name='56/560862/Crystal_structure/1'>hairpin ribozyme</scene> | In the transition state, the <scene name='56/560862/Crystal_structure/1'>hairpin ribozyme</scene> | ||
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| + | The secondary structure of the hairpin ribozyme contains two independently folding domains, called A and B. In each domain there is an internal loop flanked by two helices(H1 and H2 in domain A and H3 and H4 in domain B). The RNA substrate is bound in domain A through Watson-Crick base pairs in H1 and H2. Once bound to domain A, the substrate is reversibly cleaved. Linkers of varying lengths were inserted between the 5' end of the substrate and the 3' end of the ribozyme in order to test what proximity is preferred by the two domains. The results of the test showed that the two domains prefer to be relatively close to one another and use H2 and H3 as a sort of hinge. | ||
==References== | ==References== | ||
<references/> | <references/> | ||
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Hairpin Ribozyme Overview
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Structure
In the transition state, the
The secondary structure of the hairpin ribozyme contains two independently folding domains, called A and B. In each domain there is an internal loop flanked by two helices(H1 and H2 in domain A and H3 and H4 in domain B). The RNA substrate is bound in domain A through Watson-Crick base pairs in H1 and H2. Once bound to domain A, the substrate is reversibly cleaved. Linkers of varying lengths were inserted between the 5' end of the substrate and the 3' end of the ribozyme in order to test what proximity is preferred by the two domains. The results of the test showed that the two domains prefer to be relatively close to one another and use H2 and H3 as a sort of hinge.
References
- ↑ Fedor MJ. Structure and function of the hairpin ribozyme. J Mol Biol. 2000 Mar 24;297(2):269-91. PMID:10715200 doi:http://dx.doi.org/10.1006/jmbi.2000.3560
