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

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

doi:10.18388/abp.2014_1913

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

Ingeborg Knævelsrud Faculty of Science and Technology, Department of Mathematics and Natural Sciences-Centre for Organelle Research, University of Stavanger, Stavanger, Norway and Department of Biology and Centre for Geobiology, University of Bergen, Bergen, Norway.;
Sabina Kazazic Faculty of Science and Technology, Department of Mathematics and Natural Sciences-Centre for Organelle Research, University of Stavanger, Stavanger, Norway.;
Nils-Kåre Birkeland Department of Biology and Centre for Geobiology, University of Bergen, Bergen, Norway.;
Svein Bjelland Faculty of Science and Technology, Department of Mathematics and Natural Sciences-Centre for Organelle Research, University of Stavanger, Stavanger, Norway.;

DOI: https://doi.org/10.18388/abp.2014_1913

Abstract

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.

Published

2014-06-16

Issue

Vol. 61 No. 2 (2014)

Section

Articles

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