Characterization of an AP endonuclease from sugarcane – ScARP1.
Authors of this article are:
Cabral Medeiros NM, Córdoba-Cañero D, García-Gil CB, Ariza RR, Roldán-Arjona T, Scortecci KC.
A summary of the article is shown below:
Plants are sessile organisms that need to cope with different conditions. The Base Excision Repair (BER) pathway is an important mechanism protecting the genome from DNA lesions. Apurinic/apyrimidinic (AP) endonucleases are key BER enzymes that process AP sites arising either spontaneously or as BER intermediates. In Arabidopsis there are three AP endonucleases: AtARP1, AtAPE1L, and AtAPE2, and in sugarcane two AtARP1 homologues have been identified: ScARP1 and ScARP3. ScARP1 shares 59% sequence identity with Arabidopsis AtARP. Protein modeling of ScARP1 and AtARP1 revealed conserved active sites and metal binding sites. For biochemical characterisation, recombinant ScARP1 protein displayed AP endonuclease activity both in the presence of MnCl2 or MgCl2 and the optimal temperature for its activity was 37 °C. Under these conditions, 3′-exonuclease, 3′-phosphatase, and 3′-phosphodiesteterase activities were not detectable. We also show that ScARP1 protein is able to complement mutant atarp-/- cell extracts deficient in AP endonuclease activity. These results suggest that AP endonucleases from different plant species preserve AP endonuclease activity. The biochemical characterisation of ScARP1 extends our knowledge of the BER pathway to a monocot crop plant group.Copyright © 2019 Elsevier Inc. All rights reserved.
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This article is a good source of information and a good way to become familiar with topics such as: AP endonuclease; BER; Complementation assay; Protein expression; Saccharum spp..