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This exonuclease requires Mg 2+ in order to function and works at higher temperatures than exonuclease I. [7] Exonuclease V is a 3' to 5' hydrolyzing enzyme that catalyzes linear double-stranded DNA and single-stranded DNA, which requires Ca2+. [8] This enzyme is extremely important in the process of homologous recombination.
The protein encoded by this gene is a single-stranded DNA (ssDNA)-specific exonuclease that can slide along the DNA before cutting it. However, human replication protein A binds ssDNA and restricts sliding of the encoded protein, providing a 5'-directionality to the enzyme. This protein localizes to nuclear repair loci after DNA damage.
dnaQ is the gene encoding the ε subunit of DNA polymerase III in Escherichia coli. [1] The ε subunit is one of three core proteins in the DNA polymerase complex. It functions as a 3’→5’ DNA directed proofreading exonuclease that removes incorrectly incorporated bases during replication.
RecBCD is a model enzyme for the use of single molecule fluorescence as an experimental technique used to better understand the function of protein-DNA interactions. [23] The enzyme is also useful in removing linear DNA, either single- or double-stranded, from preparations of circular double-stranded DNA, since it requires a DNA end for activity.
[45] [15] Two amino acids required for the exonuclease function of Taq polymerase were identified by mutagenesis as arginines at positions 25 and 74 (R25 and R74). [46] A histidine to glutamic acid mutation at position 147 (short: H147E) in KOD polymerase lowers the relatively high exonuclease activity of KOD. [27]
In prokaryotes, the FEN enzyme is found as an N-terminal domain of DNA polymerase I, but some prokaryotes appear to encode a second homologue. [ 1 ] [ 2 ] [ 3 ] The endonuclease activity of FENs was initially identified as acting on a DNA duplex which has a single-stranded 5' overhang on one of the strands [ 4 ] (termed a "5' flap", hence the ...
Mol CD, Kuo CF, Thayer MM, Cunningham RP, Tainer JA (March 1995). "Structure and function of the multifunctional DNA-repair enzyme exonuclease III". Nature. 374 (6520): 381–6. doi:10.1038/374381a0. PMID 7885481. S2CID 4335526. Lahm A, Suck D (December 1991). "DNase I-induced DNA conformation. 2 A structure of a DNase I-octamer complex". J ...
The exonuclease domain contains its own catalytic site and removes mispaired bases. Among the seven different DNA polymerase families, the "palm domain" is conserved in five of these families. The "finger domain" and "thumb domain" are not consistent in each family due to varying secondary structure elements from different sequences. [9]