RNA substrate binding site in the catalytic core of the Tetrahymena ribozyme

Article Abstract:

A conserved adenine in the catalytic core contributes along with a particular ribose 2'-OH to the binding of the P1 helix, which is necessary for catalysis by group I introns. Ribozymes from Tetrahymena thermophila were analyzed using a gel-shift binding assay to learn in greater detail how the pre-ribosomal RNA intron uses a guanosine nucleophile to catalyze sequence-specific cleavage of oligonucleotides.

Binding sites (Biochemistry), Active sites (Biochemistry), Catalysis

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Metal ion catalysis in the Tetrahymena ribozyme reaction

Article Abstract:

Catalytic RNA of Tetrahymena thermophila is a metalloenzyme. This ribozyme has an absolute requirement for one of the divalent metal ions Mg2+ or Mn2+ to catalyze cleavage of exogenous RNA or DNA substrate. The presence of Mg2+ alone slows this cleavage while the addition of Mn2+ or Zn2+ speeds it about 1,000 times. The presence of Zn2+ and Mn2+ is thought to speed the reaction via coordination of sulphur.

RNA, Molecular genetics

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Peptide bond formation by in vitro selected ribozymes

Article Abstract:

Research using in vitro experiments shows that ribozymes consisting of 196 nucleotides carry out peptidyl transferase reactions also observed in the ribosome. A description of peptide bond formation by a ribosome is given and a comparison to the equivalent ribozyme reaction is made. Further research using in vitro selected ribozymes might be useful in ribosome-catalyzed protein synthesis studies.

Proteins, Protein synthesis

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