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Please use this identifier to cite or link to this item: http://repository.iitr.ac.in/handle/123456789/3937
Title: Characterization of substrate binding and enzymatic removal of a 3-methyladenine lesion from genomic DNA with TAG of MDR A. baumannii
Authors: Tomar J.S.
Narwal M.
Kumar, Pravindra R.Manish
Peddinti, Rama Krishna
Published in: Molecular BioSystems
Abstract: The rise of multiple-drug resistance in bacterial pathogens imposes a serious public health concern and has led to increased interest in studying various pathways as well as enzymes. Different DNA glycosylases collaborate during bacterial infection and disease by overcoming the effects of ROS- and RNS-mediated host innate immunity response. 3-Methyladenine DNA glycosylase I, an essential DNA repair enzyme, was chosen for the present study from the MDR species of A. baumannii. The enzyme was especially chosen because of its functional significance in A. baumannii and due to its structural variation from its human homologue. MDR strains such as A. baumannii are interesting targets owing to their evolved mechanisms of evading a host defence. In the absence of any structural information, the enzyme was characterized biophysically and biochemically. Binding studies with 3mA and Zn2+ indicated that the activity of TAG-Ab is an enthalpy-driven process. Fluorescence thermal denaturation studies described that the denaturation of TAG-Ab is a two-step process. Modified RP-HPLC-based glycosylase assay attested that the heterologously expressed and purified TAG-Ab enzyme is active and catalyses the removal of 3mA. Other binding parameters and the effect of adenine on substrate binding are also discussed in detail. © The Royal Society of Chemistry 2016.
Citation: Molecular BioSystems (2016), 12(11): 3259-3265
URI: https://doi.org/10.1039/c6mb00517a
http://repository.iitr.ac.in/handle/123456789/3937
Issue Date: 2016
Publisher: Royal Society of Chemistry
ISSN: 1742206X
Author Scopus IDs: 57191633475
49461618600
55064809000
6602375630
Author Affiliations: Tomar, J.S., Department of Chemistry, Indian Institute of Technology Roorkee, Roorkee, 247667, India
Narwal, M., Department of Biotechnology, Indian Institute of Technology Roorkee, Roorkee, 247667, India
Kumar, P., Department of Biotechnology, Indian Institute of Technology Roorkee, Roorkee, 247667, India
Peddinti, R.K., Department of Chemistry, Indian Institute of Technology Roorkee, Roorkee, 247667, India
Corresponding Author: Peddinti, R.K.; Department of Chemistry, Indian Institute of Technology RoorkeeIndia; email: rkpedfcy@iitr.ac.in
Appears in Collections:Journal Publications [CY]

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