Reverse transcriptase

Reverse transcriptase
(RNA-dependent DNA polymerase)
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]
Identifiers
SymbolRVT_1
PfamPF00078
Pfam clanCL0027
InterProIPR000477
PROSITEPS50878
SCOP21hmv / SCOPe / SUPFAM
CDDcd00304
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
RNA-directed DNA polymerase
Identifiers
EC no.2.7.7.49
CAS no.9068-38-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

A reverse transcriptase (RT) is an enzyme used to convert RNA genome 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. Contrary to a widely held belief, the process does not violate the flows of genetic information as described by the classical central dogma, as transfers of information from RNA to DNA are explicitly held possible.[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.

  1. ^ 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.
  2. ^ 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.
  3. ^ Sarkar S (1996). The Philosophy and History of Molecular Biology: New Perspectives. Dordrecht: Kluwer Academic Publishers. pp. 187–232.
  4. ^ 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.

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