Minimal Hammerhead Ribozymes with Uncompromised Catalytic Activity.

Pyrene modification leads to increased catalytic activity in minimal hammerhead ribozymes.

Highly active variants of minimal hammerhead ribozymes are generated by the replacement of substantial parts of stem-loop structures with pyrene building blocks.

Morphing the minimal and full-length hammerhead ribozymes: implications for the cleavage mechanism.

The hammerhead ribozyme is a small, intensively studied catalytic RNA, and has been used as a prototype for understanding how RNA catalysis works. In 2003, the importance of a set of tertiary contacts that appear in natural sequences of the hammerhead RNA was finally understood. The presence of these contact regions in stems I and II in 'full-length hammerhead ribozymes' is accompanied by an up...

Long-range tertiary interactions in single hammerhead ribozymes bias motional sampling toward catalytically active conformations.

Enzymes generally are thought to derive their functional activity from conformational motions. The limited chemical variation in RNA suggests that such structural dynamics may play a particularly important role in RNA function. Minimal hammerhead ribozymes are known to cleave efficiently only in ∼ 10-fold higher than physiologic concentrations of Mg(2+) ions. Extended versions containing native...

The Minimal and Full-Length Hammerhead Ribozymes: Reconciling Structure with Biochemistry

The influence of imperfectly paired helices I and III on the catalytic activity of hammerhead ribozymes.

Several catalytic antisense RNAs directed against different regions of the genomic or antigenomic RNA of Sendai virus were constructed. All RNAs contained the same catalytic domain based on hammerhead ribozymes but some had deletions or mutations resulting in imperfect helices I and III. Pre-annealed substrate/ribozyme complexes were used to determine the rates of the cleavage process for the d...