Catalytic RNA by T. R. Cech, D. Herschlag (auth.), Professor Dr. Fritz

By T. R. Cech, D. Herschlag (auth.), Professor Dr. Fritz Eckstein, Professor David M. J. Lilley (eds.)

In contemporary years, unheard of advances in lots of facets of the molecular biology of nucleic acids were witnessed. the realm of RNA chemistry has gone through one of those explosion, with a massive curiosity in RNA-mediated catalysis. while, our structural figuring out of DNA-protein interactions has elevated tremendously, and the comparable region of RNA-protein interactions is commencing to assemble speed. This softcover variation from the winning sequence Nucleic Acids and Molecular Biology is dedicated to the constitution and mechanism of ribozymes, and their capability exploitation. the topic has either very important evolutionary implications and capability functional software within the improvement of healing brokers for ailments akin to AIDS.

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1993). This quenching is apparently due to electron transfer (O'Connor et al. 1994; Netzel et al. 1995; Manoharan et al. 1996). The fluorescence of lOA can change by twofold upon binding (Sugimoto et al. 1989b). Fig. 2 provides an example of the wealth of data available from a single shot in a rapid mixing apparatus employing fluorescence detection. In this experiment, pyrCCUCUA was mixed with the group I ribozyme, L-21 Scal, in the presence of pG. Collection of a total of 500 time points over two separate time windows of 10 and 100s permitted detection of three separate fluorescence transients.

In the second step, a conformational change is necessary for positioning the last nucleotide of the intron, always a guanosine, in the guanosine-binding site in a conformation similar to that of the free guanosine cofactor (Figs. 1,2; Sect. 4). 0 and PI0 (see Sect. 4). These interactions bring the phosphodiester bond between the terminal G and the 3' exon next to the 3' OR attacking group of the 5' exon, resulting in the ligation of the exons. The splicing mechanism can be seen as a dynamic process in which the catalytic core of the group I intron must successively 3' Fig.

More detailed experiments with 32P-labeled substrates have shown coupled binding between oligopyrimidine substrates and pG (McConnell et al. 1993). Interestingly, fluorescence studies show that the coupled binding is dependent on the 2'OH group of pG (Bevilacqua et al. 1993; Y. Li, L. Profenno, R. H. Turner, unpubl. experiments). For example, compared with the absence of cofactor, pyrCUCU binds four- Fig. 7. A speculative model for the interaction of pG with eeUeUA at the catalytic site of the group I ribozyme, L-21 Sca I.

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