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Fusing an open reading frame on either side of pfu polymerase does not affect its activity
Author(s) -
Rashid Mohammad,
Nayeem Syed
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.895.15
Subject(s) - polymerase , enzyme , fusion protein , open reading frame , dna polymerase , recombinant dna , biology , biochemistry , microbiology and biotechnology , chemistry , gene , peptide sequence
Fusion protein constructs based on genetic engineering could be useful in obtaining efficient fusion enzymes with dual function that is also cost effective. However, fusing two long open reading frames may be cumbersome in terms of producing a functional hybrid enzyme having two distinct domains. Here, we have been trying to fuse a pfu DNA polymerase enzyme of 90 kDa with a pfu dUTPase enzyme of 26 kDa. Fusing the dUTPase on either amino‐ or carboxyl‐terminal of DNA polymerase does not affect the polymerase activity of the enzyme in crude as well as in purified version of the hybrid enzyme. However, dUTPase function is yet to be analyzed in the fusion protein that would be the ultimate goal of this project.