By Valentin V. Vlassov, Marina A. Zenkova (auth.), Dr. Marina A. Zenkova (eds.)

The improvement of brokers in a position to cleaving RNA and DNA has attracted massive consciousness of researchers within the previous few years, due to their software in biotechnology and pharmacology. synthetic nucleases are rationally designed to mimic the lively facilities of ordinary enzymes by way of uncomplicated buildings owning minimum units of an important features which are crucial for catalysis. Being much less effective and particular than average enzymes, the primitive mimics are smaller, extra strong and ready to functionality in a extensive diversity of stipulations.

The authors of the current quantity summarize the cutting-edge within the speedily constructing box of man-made nucleases. The chapters care for mechanisms of RNA and DNA cleavage via chemical brokers and ordinary enzymes, improvement of latest nucleic acid-cleaving brokers, functions of man-made nucleases, and layout of oligonucleotide conjugates with RNA- and DNA-cleaving agents.

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This substitution decreases the value of kca/KM by lQz-fold for the cleavage of poly(C) and UpA. Unlike an alanine residue, an asparagine residue can favor formation of a hydrogen bond to the leaving group in the transition state. One interpretation of these data is that such a hydrogen bond enhances the affinity of the enzyme for the rate-limiting transition state by 10z-fold. His12 and Hisl19 not only play an important role in catalysis by RNase A, but also contribute to the binding of single-stranded nucleic acids (Park et al.

The experiments described above raise the question of how long a singlestranded RNA fragment has to be in order to undergo specific cleavage. To answer this question, the stability of GCUCGUAA was tested when paired with each of four different complementary oligoribonucleotides (Bibillo et al. 1999a). The first complementary oligomer, UUACGAGC, is able to form a perfect duplex with the studied octamer. The three following oligomers: UACGAGC,ACGAGC, and CGAGC are one, two, and three nucleotides shorter, respectively, at the 5' -end.

This effect has been examined in detail with enzymatic assays that monitor the cleavage of 6-carboxytetramethylrhodamine-dArU( dA)2-6-carboxyfluorescein (6-TAMRA-dArU( dA)2 -6-FAM), which is a fluorogenic substrate in which a labile ribonucleotide residue is embedded between three deoxynucleotide residues (Kelemen et al. 1999). Unlike shorter substrates, 6-TAMRA-dArU(dA)2-6-FAM can interact with all of the known phosphoryl-group binding sites of RNase A. 0 M NaCl (Fig. 4). 010 M NaCl, this value increases to 3x109 M-1 S-l, which is among the largest known for an enzyme.

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