Polymerase

A polymerase is an enzyme (EC 2.7.7.6/7/19/48/49) that synthesizes long chains of polymers or nucleic acids. DNA polymerase and RNA polymerase are used to assemble DNA and RNA molecules, respectively, by copying a DNA template strand using base-pairing interactions or RNA by half ladder replication.

Structure of Taq DNA polymerase

A DNA polymerase from the thermophilic bacterium, Thermus aquaticus (Taq) (PDB 1BGX, EC 2.7.7.7) is used in the polymerase chain reaction, an important technique of molecular biology.

A polymerase may be template dependent or template independent. Poly-A-polymerase is an example of template independent polymerase. Terminal deoxynucleotidyl transferase also known to have template independent and template dependent activities.

Types

In general, viral single-subunit RNA polymerases/replicases/reverse transcriptase shares a common origin with DNA polymerase. They have a conserved "palm" domain.[2] Multi-subunit RNA polymerase forms an unrelated group.[3] Primases have a more complex story: bacterial primases with the Toprim domain are related to topoisomerase and mitochrondrial helicase,[4] while archaea and eukaryotic primases form an unrelated family, possibly related to the polymerase palm. Both families nevertheless associate to the same bunch of helicases.[5]

Classes of Template dependent polymerase
DNA-polymerase RNA-polymerase
Template is DNA DNA dependent DNA-polymerase
or common DNA polymerases
DNA dependent RNA-polymerase
or common RNA polymerases
Template is RNA RNA dependent DNA polymerase
or Reverse transcriptase
RNA dependent RNA polymerase
or RdRp or RNA-replicase

See Also

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References

  1. Loc'h, Jérôme (2016). "Structural Basis for a New Templated Activity by Terminal Deoxynucleotidyl Transferase: Implications for V(D)J Recombination". Structure. 24 (9): 1452–1463. doi:10.1016/j.str.2016.06.014. PMID 27499438.
  2. Hansen JL, Long AM, Schultz SC (August 1997). "Structure of the RNA-dependent RNA polymerase of poliovirus". Structure. 5 (8): 1109–22. doi:10.1016/S0969-2126(97)00261-X. PMID 9309225.
  3. Cramer, P (February 2002). "Multisubunit RNA polymerases". Current Opinion in Structural Biology. 12 (1): 89–97. doi:10.1016/S0959-440X(02)00294-4. PMID 11839495.
  4. Aravind, L; Leipe, DD; Koonin, EV (15 September 1998). "Toprim--a conserved catalytic domain in type IA and II topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins". Nucleic Acids Research. 26 (18): 4205–13. doi:10.1093/nar/26.18.4205. PMC 147817. PMID 9722641.
  5. Iyer, LM; Koonin, EV; Leipe, DD; Aravind, L (2005). "Origin and evolution of the archaeo-eukaryotic primase superfamily and related palm-domain proteins: structural insights and new members". Nucleic Acids Research. 33 (12): 3875–96. doi:10.1093/nar/gki702. PMC 1176014. PMID 16027112.
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