Characterization of an AP endonuclease from sugarcane - ScARP1.

Autor: Cabral Medeiros NM; Laboratório de Transformação de Plantas e Microscopia (LTPM), Departamento de Biologia Celular e Genética, Centro de Biociências, Universidade Federal do Rio Grande do Norte, Brazil; Programa de Pós-Graduação em Bioquímica da Universidade Federal do Rio Grande do Norte, Spain., Córdoba-Cañero D; Instituto Maimónides de Investigación Biomédica de Córdoba (IMIBIC), Spain; Universidad de Córdoba, Spain; Hospital Universitario Reina Sofía, Spain., García-Gil CB; Instituto Maimónides de Investigación Biomédica de Córdoba (IMIBIC), Spain; Universidad de Córdoba, Spain; Hospital Universitario Reina Sofía, Spain., Ariza RR; Instituto Maimónides de Investigación Biomédica de Córdoba (IMIBIC), Spain; Universidad de Córdoba, Spain; Hospital Universitario Reina Sofía, Spain., Roldán-Arjona T; Instituto Maimónides de Investigación Biomédica de Córdoba (IMIBIC), Spain; Universidad de Córdoba, Spain; Hospital Universitario Reina Sofía, Spain., Scortecci KC; Laboratório de Transformação de Plantas e Microscopia (LTPM), Departamento de Biologia Celular e Genética, Centro de Biociências, Universidade Federal do Rio Grande do Norte, Brazil; Programa de Pós-Graduação em Bioquímica da Universidade Federal do Rio Grande do Norte, Spain. Electronic address: kacscort@yahoo.com.
Jazyk: angličtina
Zdroj: Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2019 Jun 30; Vol. 514 (3), pp. 926-932. Date of Electronic Publication: 2019 May 10.
DOI: 10.1016/j.bbrc.2019.04.156
Abstrakt: 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 MnCl 2 or MgCl 2 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.)
Databáze: MEDLINE
Externí odkaz: