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, unparalleled advances in lots of features of the molecular biology of nucleic acids were witnessed. the realm of RNA chemistry has passed through one of those explosion, with a massive curiosity in RNA-mediated catalysis. whilst, our structural knowing of DNA-protein interactions has elevated significantly, and the comparable sector of RNA-protein interactions is commencing to assemble velocity. This softcover variation from the profitable sequence Nucleic Acids and Molecular Biology is dedicated to the constitution and mechanism of ribozymes, and their strength exploitation. the topic has either vital evolutionary implications and strength sensible software within the improvement of healing brokers for ailments similar to AIDS.

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Mechanism of self-splicing in the context of the three-dimensional model of the group I intron core. The drawings are based on the view that natural group I introns are composed of a static, stable ribozyme moiety (green and violet) and a succession of substrates: the guanosine cofactor (orange arrow), the PI helix formed by the internal guide sequence (red) binding the 5' exon (black), and the 3' splice site (yellow) with the 3' exon (black). From left to right. In the first step of the reaction, the guanosine cofactor cuts the 5' exon-intron junction.

1994). As suggested by comparative sequence analysis and confirmed experimentally by site-directed mutagenesis, in vitro genetics and NMR, this coaxial stacking is favored by the formation of small triple helices between the strand leaving P6 and the major groove of P4 and the strand entering P4 and the minor groove of helix P6 (Michel and Westhof 1990; Michel et al. 1990a; Chastain and Tinoco 1992, 1993; Green and Szostak 1994). Because these triple helices dictate the direction of the leaving and entering strands, they are likely to govern the orientation of the P4-P6 domain in relation to the P3-P8 domain (Figs.

Secondary structural elements form the first level of structural organization and they are also the last pairings to break at high temperatures (Banerjee et al. 1993; Jaeger et al. 1993). Site-specific mutagenesis and chemical and enzymatic probing confirm the existence of all the pairings within the active structure of group I introns (Cech 1993). The next level of organization leads to the stacking of adjacent helices such as P4 and P6 or P3 and P8. The stacking of P4 and P6 was verified experimentally for the P4-P6 domain, simultaneously corroborating the view of the P4, P5, and P6 helices as part of an independent folding domain in the Tetrahymena intron (Murphy and Cech 1993; Murphy et al.

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