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Using structural-based protein engineering to modulate the differential inhibition effects of SAUGI on human and HSV uracil DNA glycosylase.

Wang HC, Ho CH, Chou CC, Ko TP, Huang MF, Hsu KC, Wang AH
Nucleic Acids Res 44 4440-9 (2016)
Cited: 7 times
EuropePMC logo PMID: 26980279

Abstract

Uracil-DNA glycosylases (UDGs) are highly conserved proteins that can be found in a wide range of organisms, and are involved in the DNA repair and host defense systems. UDG activity is controlled by various cellular factors, including the uracil-DNA glycosylase inhibitors, which are DNA mimic proteins that prevent the DNA binding sites of UDGs from interacting with their DNA substrate. To date, only three uracil-DNA glycosylase inhibitors, phage UGI, p56, and Staphylococcus aureus SAUGI, have been determined. We show here that SAUGI has differential inhibitory effects on UDGs from human, bacteria, Herpes simplex virus (HSV; human herpesvirus 1) and Epstein-Barr virus (EBV; human herpesvirus 4). Newly determined crystal structures of SAUGI/human UDG and a SAUGI/HSVUDG complex were used to explain the differential binding activities of SAUGI on these two UDGs. Structural-based protein engineering was further used to modulate the inhibitory ability of SAUGI on human UDG and HSVUDG. The results of this work extend our understanding of DNA mimics as well as potentially opening the way for novel therapeutic applications for this kind of protein.

Articles - 5ayr mentioned but not cited (1)

  1. Using structural-based protein engineering to modulate the differential inhibition effects of SAUGI on human and HSV uracil DNA glycosylase. Wang HC, Ho CH, Chou CC, Ko TP, Huang MF, Hsu KC, Wang AH. Nucleic Acids Res 44 4440-4449 (2016)


Reviews citing this publication (3)

  1. New paradigm of functional regulation by DNA mimic proteins: Recent updates. Wang HC, Chou CC, Hsu KC, Lee CH, Wang AH. IUBMB Life 71 539-548 (2019)
  2. Focus on DNA Glycosylases-A Set of Tightly Regulated Enzymes with a High Potential as Anticancer Drug Targets. Hans F, Senarisoy M, Bhaskar Naidu C, Timmins J. Int J Mol Sci 21 E9226 (2020)
  3. The Essential Co-Option of Uracil-DNA Glycosylases by Herpesviruses Invites Novel Antiviral Design. Savva R. Microorganisms 8 E461 (2020)

Articles citing this publication (3)

  1. Herpes Simplex Virus 1 UL2 Inhibits the TNF-α-Mediated NF-κB Activity by Interacting With p65/p50. Cai M, Liao Z, Zou X, Xu Z, Wang Y, Li T, Li Y, Ou X, Deng Y, Guo Y, Peng T, Li M. Front Immunol 11 549 (2020)
  2. The monomeric form of Neisseria DNA mimic protein DMP19 prevents DNA from binding to the histone-like HU protein. Huang MF, Lin SJ, Ko TP, Liao YT, Hsu KC, Wang HC. PLoS One 12 e0189461 (2017)
  3. Identification and Mechanism of Action of the Global Secondary Metabolism Regulator SaraC in Stereum hirsutum. Hu QY, Pu XJ, Li GH, Li CQ, Lei HM, Zhang KQ, Zhao PJ. Microbiol Spectr 10 e0262422 (2022)


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