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DNA polymerase I information


DNA polymerase I
Functional domains in the Klenow Fragment (left) and DNA Polymerase I (right).
Identifiers
OrganismEscherichia coli
(str. K-12 substr. MG1655)
SymbolpolA
Entrez948356
PDB1DPI
RefSeq (Prot)NP_418300.1
UniProtP00582
Other data
EC number2.7.7.7
Chromosomegenome: 4.04 - 4.05 Mb
Search for
StructuresSwiss-model
DomainsInterPro

DNA polymerase I (or Pol I) is an enzyme that participates in the process of prokaryotic DNA replication. Discovered by Arthur Kornberg in 1956,[1] it was the first known DNA polymerase (and the first known of any kind of polymerase). It was initially characterized in E. coli and is ubiquitous in prokaryotes. In E. coli and many other bacteria, the gene that encodes Pol I is known as polA. The E. coli Pol I enzyme is composed of 928 amino acids, and is an example of a processive enzyme — it can sequentially catalyze multiple polymerisation steps without releasing the single-stranded template.[2] The physiological function of Pol I is mainly to support repair of damaged DNA, but it also contributes to connecting Okazaki fragments by deleting RNA primers and replacing the ribonucleotides with DNA.

  1. ^ Lehman IR, Bessman MJ, Simms ES, Kornberg A (July 1958). "Enzymatic synthesis of deoxyribonucleic acid. I. Preparation of substrates and partial purification of an enzyme from Escherichia coli". The Journal of Biological Chemistry. 233 (1): 163–70. doi:10.1016/S0021-9258(19)68048-8. PMID 13563462.
  2. ^ Voet D, Voet JG, Pratt CW (1999). Fundamentals of Biochemistry. New York: Wiley.[page needed]

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are ultimately replaced with DNA bases by RNase H nuclease (eukaryotes) or DNA polymerase I nuclease (prokaryotes). DNA Ligase then acts to join the two...

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