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Polynucleotide analogs template

There are two possible mechanisms by which a polynucleotide analog can inhibit the polymerase in the template-specific manner. Polynucleotide analogs can displace polymerase from its template and release the enzyme into solution in a free form alternatively, the polymerase can become blocked on the template polynucleotide analog complex and remain there in a bound, inactive form. These alternatives were investigated for two enzymes, alpha class DNA polymerase and E. colt RNA polymerase. In both cases the polymerase becomes blocked on the polynucleotide templates rather than being released in free form ... [Pg.7]

Specific inhibition of templated biosynthesis by electroneutral polynucleotide analogs can be achieved even with complex templates Messenger RNA coding for globin, similarly to other messenger RNA molecules, contains a polyadenylate sequence located... [Pg.7]

Template-directed oligonucleotide synthesis in the presence of synthetic cationic polynucleotide analogs... [Pg.324]

The present study, the template-directed oligonucleotide synthesis, showed a considerable selection of monomers with the aid of such specific base-base interaction. In the preceding trials for template-directed oligonucleotide syntheses, neutral or anionic polynucleotides or polynucleotide analogs were utilized as template molecules However, because of the low affinity between template molecules and mononucleotides, owing to a disadvantage of... [Pg.324]

The most essential point for the template-directed oligonucleotide synthesis is the selective interaction of monomers with the template molecules. As was discussed in 2-1., water-soluble cationic polynucleotide analogs interacted significantly with mononucleotides at relatively low base concentration (-10 > 10 Vol dm ) and the mode of the base-base interaction was dominantly the vertical stacking. In contrast, the base-base interaction in the heterogeneous... [Pg.331]

Template-directed condensation of nucleotide in the presence of polynucleotide analog ... [Pg.333]

The inhibitions described above occurred only when the analog and polynucleotide contained complementary bases. These combinations are not the only ones in which the interaction can occur, e.g., affinity methods detect some interaction between the non-complementary poly-9-vinyladenine and polyadenylate Apparently, such complexes are too unstable to affect the enzymatic reactions nevertheless, extensive modification of the analog can increase the stability of the polymer-polynucleotide complex to the point where such a polymer can effectively inhibit the reaction. Thus, omisssion of the amino group from poly-9-vinyladenine leads to poly-9-vinylpurine and the latter polymer inhibits the reverse transcription of polyadenylate and polyuridylate The introduction of a dimethylamino group in place of the amino group of poly-9-vinyladenine abolMies all of its inhibitory effects All these effects can be correlated with the ability of polymers to form complexes with templates. [Pg.8]

The general conclusions derived from these experiments are a) electroneutral analogs of polynucleotides cannot function as templates of enzymatic... [Pg.6]

The synthesis of RNA is analogous in many ways to the synthesis of DNA, with the chain growing in the 5 3 direction. As distinct from the latter, however, which appears to be manufactured only at cell division, the synthesis of m-RNA takes place continuously. This is directed by a DNA strand which acts as a template, and needs the aid of the enzyme RNA polymerase. The incoming nncleo-side triphosphates (with bases A, C, G and U) polymerise to form a polynucleotide chain, and in this process they arrange themselves in sequence complimentary to the sequence of A, C, G and T in one of the strands of DNA already present. [Pg.993]


See other pages where Polynucleotide analogs template is mentioned: [Pg.1]    [Pg.4]    [Pg.4]    [Pg.6]    [Pg.7]    [Pg.7]    [Pg.12]    [Pg.15]    [Pg.1]    [Pg.4]    [Pg.4]    [Pg.6]    [Pg.7]    [Pg.7]    [Pg.9]    [Pg.12]    [Pg.15]    [Pg.315]    [Pg.324]    [Pg.325]    [Pg.330]    [Pg.334]    [Pg.336]    [Pg.8]    [Pg.199]    [Pg.1104]    [Pg.989]    [Pg.456]    [Pg.458]    [Pg.103]    [Pg.204]    [Pg.205]    [Pg.205]   
See also in sourсe #XX -- [ Pg.315 ]




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