Reverse transcriptase (RNA-dependent DNA polymerase) |
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Crystallographic structure of HIV-1 reverse transcriptase where the two subunits p51 and p66 are colored and the active sites of polymerase and nuclease are highlighted. [1] |
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| Symbol | RVT_1 |
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| Pfam | PF00078 |
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| Pfam clan | CL0027 |
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| InterPro | IPR000477 |
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| PROSITE | PS50878 |
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| SCOP2 | 1hmv / SCOPe / SUPFAM |
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| CDD | cd00304 |
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A reverse transcriptase (RT) is an enzyme used to convert RNA to DNA, a process termed reverse transcription. Reverse transcriptases are used by viruses such as HIV and hepatitis B to replicate their genomes, by retrotransposon mobile genetic elements to proliferate within the host genome, and by eukaryotic cells to extend the telomeres at the ends of their linear chromosomes. The process does not violate the flows of genetic information as described by the classical central dogma, but rather expands it to include transfers of information from RNA to DNA.[2][3][4]
Retroviral RT has three sequential biochemical activities: RNA-dependent DNA polymerase activity, ribonuclease H (RNase H), and DNA-dependent DNA polymerase activity. Collectively, these activities enable the enzyme to convert single-stranded RNA into double-stranded cDNA. In retroviruses and retrotransposons, this cDNA can then integrate into the host genome, from which new RNA copies can be made via host-cell transcription. The same sequence of reactions is widely used in the laboratory to convert RNA to DNA for use in molecular cloning, RNA sequencing, polymerase chain reaction (PCR), or genome analysis.
- ^ PDB: 3KLF; Tu X, Das K, Han Q, Bauman JD, Clark AD, Hou X, Frenkel YV, Gaffney BL, Jones RA, Boyer PL, Hughes SH, Sarafianos SG, Arnold E (October 2010). "Structural basis of HIV-1 resistance to AZT by excision". Nature Structural & Molecular Biology. 17 (10): 1202–9. doi:10.1038/nsmb.1908. PMC 2987654. PMID 20852643.
- ^ Crick F (August 1970). "Central dogma of molecular biology". Nature. 227 (5258): 561–3. Bibcode:1970Natur.227..561C. doi:10.1038/227561a0. PMID 4913914. S2CID 4164029.
- ^ Sarkar S (1996). The Philosophy and History of Molecular Biology: New Perspectives. Dordrecht: Kluwer Academic Publishers. pp. 187–232.
- ^ Danchin É, Pocheville A, Rey O, Pujol B, Blanchet S (2019). "Epigenetically facilitated mutational assimilation: epigenetics as a hub within the inclusive evolutionary synthesis". Biological Reviews. 94 (1): 259–282. doi:10.1111/brv.12453. PMC 6378602. S2CID 67861162.