Abstract
The role of individual functional groups on cytidine 17 in the hammerhead ribozyme was assessed by introducing modified pyrimidines into two kinetically well-characterized hammerheads. As long as the pyrimide ring size was maintained, the modifications had no effect on substrate binding, suggesting that the C17-C3 hydrogen bond observed in the X-ray structure is energetically neutral. However, modification of the exocyclic amino group and the cerbonyl of C17 reduced the cleavage rate significantly, indicating that these groups are important in stabilizing the transition-state structure. C17 modifications did not affect the ratio of the forward and reverse reaction rates. Thus, unlike that believed previously, C17 is another one of many hammerhead residues critical in maintaining iIts active structure.
Original language | English (US) |
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Pages (from-to) | 1135-1142 |
Number of pages | 8 |
Journal | RNA |
Volume | 3 |
Issue number | 10 |
State | Published - Oct 1997 |
Keywords
- Catalytic RNA
- Ribozyme
- Structure-function
ASJC Scopus subject areas
- Molecular Biology