![]() coli resides on a separate protein structural domain. These data are consistent with the hypothesis that each of the three enzymatic activities of DNA polymerase I from E. Noncanonical DNA structures that stall DNA replication can cause errors in genomic DNA. It retains polymerase activity, but lacks both 5’ > 3’ and 3' > 5’ exonuclease activity. We find that the C-terminal domain has polymerase activity (albeit at a lower specific activity than the native Klenow fragment) but no measurable 3'-5' exonuclease activity. Klenow Fragment (3'5' exo-) DNA Pol I, Large (Klenow) fragment was originally derived as a proteolytic product of E. ![]() To test this hypothesis, we have cloned the DNA coding for the large domain into an expression system and purified the protein product. ![]() coli DNA Polymerase I which retains polymerization and 3 5 exonuclease activity, but has lost 5 3 exonuclease activity (1). Several lines of evidence suggested that the large domain also contains the polymerase active site. Elucidation of the metal-binding properties of the Klenow fragment of Escherichia coli polymerase I and bacteriophage T4 DNA polymerase by lanthanide(III) luminescence spectroscopy. DNA Polymerase I, Large (Klenow) Fragment is a proteolytic product of E. The larger C-terminal domain contains a deep cleft that is believed to bind duplex DNA. coli Polymerase I DNA-dependent repair enzyme. The smaller domain has a binding site for deoxynucleoside monophosphate and a divalent metal ion that is thought to identify the 3'-5' exonuclease active site. Klenow Fragment is a mesophilic DNA polymerase derived from the E. The crystal structure showed that the fragment is folded into two distinct domains. The Klenow fragment of DNA polymerase I from Escherichia coli has two enzymatic activities: DNA polymerase and 3'-5' exonuclease.
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