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Structure of Taq DNA 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.

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.

TypesEdit

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 a unrelated family, possibly related to the polymerase palm. Both families nevertheless associate to the same bunch of helicases.[5]

ReferencesEdit

  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.