The pH optimum of native uracil-DNA glycosylase of Archaeoglobus fulgidus compared to recombinant enzyme indicates adaption to cytosolic pH. | Zendy

Ingeborg Knævelsrud | Zendy; Sabina Kazazic | Zendy; Nils-Kåre Birkeland | Zendy; Svein Bjelland | Zendy

Open Access

The pH optimum of native uracil-DNA glycosylase of Archaeoglobus fulgidus compared to recombinant enzyme indicates adaption to cytosolic pH.

Author(s) -

Ingeborg Knævelsrud,

Sabina Kazazic,

Nils-Kåre Birkeland,

Svein Bjelland

Publication year - 2014

Publication title -

acta biochimica polonica

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.452

H-Index - 78

eISSN - 1734-154X

pISSN - 0001-527X

DOI - 10.18388/abp.2014_1913

Subject(s) - recombinant dna , uracil dna glycosylase , biochemistry , uracil , enzyme , cytosol , dna glycosylase , chemistry , escherichia coli , dna , cytoplasm , biology , microbiology and biotechnology , gene , dna repair

Uracil-DNA glycosylase of Archaeoglobus fulgidus (Afung) in cell extracts exhibited maximal activity around pH 6.2 as compared to pH 4.8 for the purified recombinant enzyme expressed in Escherichia coli. Native Afung thus seems to be adapted to the intracellular pH of A. fulgidus, determined to be 7.0±0.1. Both recombinant and native Afung exhibited a broad temperature optimum for activity around 80°C, reflecting the A. fulgidus optimal growth temperature of 83°C. Adaption to the neutral conditions in the A. fulgidus cytoplasm might be due to covalent modifications or accessory factors, or due to a different folding when expressed in the native host.

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