Functional analysis on a naturally occurring variant of the Staphylococcus Aureus uracil DNA Glycosylase inhibitor

Veronika Papp-Kádár, Zoltán Balázs, Gergely N. Nagy, Tünde Juhász, Károly Liliom, Beáta G. Vértessy

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Repair of DNA damage relies on various pathways including the base excision repair (BER) which targets erroneous bases in the DNA. Here, Uracil-DNA glycosylases (UDGs) are responsible for recognition and removal of uracil base from the DNA. Here, we characterize the interaction of Staphylococcus aureus UDG (SAUDG) with a naturally occurring variant of S. aureus uracil-DNA glycosylase inhibitor (SAUGI). This variant contains a histidine instead of a glutamate at the 24th position which affects the SAUDG:SAUGI interaction surface. We assessed the complex formation of SAUDG with these two SAUGI variants by independent biophysical methods. Our data reveal that the residue difference at the 24th position does not have a marked effect on the binding affinity, yet it confers alteration of the thermodynamics of the interaction. We propose that the E24H variant of SAUGI allows efficient complex formation, and consequently, inhibition of SAUDG.

Original languageEnglish
Pages (from-to)51-56
Number of pages6
JournalPeriodica Polytechnica Chemical Engineering
Volume62
Issue number1
DOIs
Publication statusPublished - Dec 1 2018

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Keywords

  • Base excision repair
  • DNA repair
  • Uracil-DNA glycosylase inhibitor

ASJC Scopus subject areas

  • Chemical Engineering(all)

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