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Folding and Activity of the Hammerhead Ribozyme
Author(s) -
Hammann Christian,
Lilley David M. J.
Publication year - 2002
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20020802)3:8<690::aid-cbic690>3.0.co;2-c
Subject(s) - hammerhead ribozyme , ribozyme , vs ribozyme , hairpin ribozyme , folding (dsp implementation) , computational biology , mammalian cpeb3 ribozyme , chemistry , biology , biochemistry , rna , gene , engineering , electrical engineering
The hammerhead is the smallest of the nucleolytic ribozymes, that undergo backbone cleavage by a transesterification reaction in the presence of magnesium ions. The RNA is induced to fold into its active conformation by the binding of metal ions in two stages. These generate domain 2, the scaffold on which the ribozyme is built, and domain 1, the active centre of the ribozyme. Further local structural rearrangement during the activation of the ribozyme is suggested by a number of crystal structures. The 10 5 ‐fold rate enhancement is probably brought about by a combination of metal‐ion participation and stereochemical factors in the environment of the folded RNA structure.