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Reverse transcriptase
(redirected from Hiv-1 reverse transcriptase)

   Also found in: Medical, Wikipedia 0.06 sec.
Reverse transcriptase

Any of the deoxyribonucleic acid (DNA) polymerases present in particles of retroviruses which are able to carry out DNA synthesis using an RNA template. This reaction is called reverse transcription since it is the opposite of the usual transcription reaction, which involves RNA synthesis using a DNA template. See Retrovirus

The transfer of genetic information from RNA to DNA in retrovirus replication was proposed in 1964 by H. M. Temin in the DNA provirus hypothesis for the replication of Rous sarcoma virus, an avian retrovirus which causes tumors in chickens and transformation of cells in culture, and reverse transcriptase has since been purified from virions of many retroviruses. The avian, murine, and human retrovirus DNA polymerases have been extensively studied.

Studies indicate that reverse transcriptase is widely distributed in living organisms and that all reverse transcriptases are evolutionarily related. For example, the organization of the nucleotide sequence of integrated retroviral DNA has a remarkable resemblance to the structure of bacterial transposable elements, in particular, transposons.

Reverse transcriptase genes are present in the eukaryotic organisms in retrotransposons and in retroposons or long interspersed (LINE) elements. Both of these types of elements can transpose in cells. See Deoxyribonucleic acid (DNA), Ribonucleic acid (RNA), Transposons



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spectroscopy, and small-angle X-ray-scattering techniques, they can reveal the makeup of molecules and materials as diverse as the human cold virus, the enzyme HIV-1 reverse transcriptase, some high-temperature superconductors, and many crystals.
The first gene silenced codes for the enzyme, HIV-1 reverse transcriptase, which is used by the virus to convert its RNA into DNA, which can then be incorporated into the genome of the infected human host.
One study, which analyzed the crystal structure of HIV-1 reverse transcriptase bound to tenofovir, revealed that the unique acyclic chemical structure of tenofovir might contribute to the infrequency of cross-resitance and resistance development.
 
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