- Hairpin ribozyme
The hairpin ribozyme is a small section of
RNA that can act as an enzyme known as aribozyme . Like thehammerhead ribozyme it is found in RNA satellites of plant viruses. It was first identified in the minus strand of the tobacco ringspot virus (TRSV) satellite RNA where it catalyzes a self-cleavage reaction to process the products of rolling circle virus replication to unit-length satellite RNA. Unlike other ribozymes that cleave RNA the hairpin ribozyme does not require a metal ion for the reaction.tructure
The structure of the hairpin ribozyme has been solved by
x-ray crystallography . The minimal hairpin ribozyme structure required for self-cleavage is composed of fourbase pair ed helices, and 2 internal loops, A and B. The bond that is cleaved lies within loop A.pecies distribution
The hairpin ribozyme has been identified in only 3 plant satellite RNAs:
*tobacco ringspot virus (TRSV)
* chicory yellow mottle virus (CYMV)
*arabis mosaic virus (ARMV)References
* [1] cite journal | last = Butcher | first = SE | coauthors = Burke JM | year = 1994 | title = Structure-mapping of the hairpin ribozyme. Magnesium-dependent folding and evidence for tertiary interactions within the ribozyme-substrate complex | journal = J Mol Biol | volume = 244 | pages = 52–63 | pmid = 7966321 | doi = 10.1006/jmbi.1994.1703
* [2] cite journal | last = Symons | first = RH | year = 1997 | title = Plant pathogenic RNAs and RNA catalysis | journal = Nucleic Acids Res | volume = 25 | pages = 2683–2689 | pmid = 9207012 | doi = 10.1093/nar/25.14.2683
* [3] cite journal | last = Doherty | first = EA | coauthors = Doudna JA | year = 2001 | title = Ribozyme structures and mechanisms | journal = Annu Rev Biophys Biomol Struct | volume = 30 | pages = 457–475 | pmid = 11441810 | doi = 10.1146/annurev.biophys.30.1.457
* [4] cite journal | last = Ferre-D'amare | first = AR | coauthors = Rupert PB | year = 2002 | title = The hairpin ribozyme: from crystal structure to function | journal = Biochem Soc Trans | volume = 30 | pages = 1105–1109 | pmid = 12440983 | doi = 10.1042/BST0301105External links
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