Endonuclease III-like protein 1

Definition:

Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines. Has also 8-oxo-7,8-dihydroguanine (8-oxoG) DNA glycosylase activity. Acts preferentially on DNA damage opposite guanine residues in DNA. Is able to process lesions in nucleosomes without requiring or inducing nucleosome disruption.

References:

[1]. M Dizdaroglu, et al. Excision of products of oxidative DNA base damage by human NTH1 protein. Biochemistry. 1999 Jan 5;38(1):243-6. [Content Brief]

[2]. Xiang Liu, et al. Truncation of amino-terminal tail stimulates activity of human endonuclease III (hNTH1). J Mol Biol. 2002 Aug 9;321(2):265-76. [Content Brief]

[3]. L Eide, et al. Human endonuclease III acts preferentially on DNA damage opposite guanine residues in DNA. Biochemistry. 2001 Jun 5;40(22):6653-9. [Content Brief]

[4]. Ian D Odell, et al. Nucleosome disruption by DNA ligase III-XRCC1 promotes efficient base excision repair. Mol Cell Biol. 2011 Nov;31(22):4623-32. [Content Brief]

[5]. Izumi Miyabe, et al. Identification of 5-formyluracil DNA glycosylase activity of human hNTH1 protein. Nucleic Acids Res. 2002 Aug 1;30(15):3443-8. [Content Brief]

[6]. Naoyuki Matsumoto, et al. Fluorescent probes for the analysis of DNA strand scission in base excision repair. Nucleic Acids Res. 2010 Apr;38(7):e101. [Content Brief]

[7]. Dina R Marenstein, et al. Substrate specificity of human endonuclease III (hNTH1). Effect of human APE1 on hNTH1 activity. J Biol Chem. 2003 Mar 14;278(11):9005-12. [Content Brief]

[8]. R Aspinwall, et al. Cloning and characterization of a functional human homolog of Escherichia coli endonuclease III. Proc Natl Acad Sci U S A. 1997 Jan 7;94(1):109-14. [Content Brief]

[9]. Amalthiya Prasad, et al. Initiation of base excision repair of oxidative lesions in nucleosomes by the human, bifunctional DNA glycosylase NTH1. Mol Cell Biol. 2007 Dec;27(24):8442-53. [Content Brief]

[10]. T P Hilbert, et al. Cloning and expression of the cDNA encoding the human homologue of the DNA repair enzyme, Escherichia coli endonuclease III. J Biol Chem. 1997 Mar 7;272(10):6733-40. [Content Brief]

[11]. Atsushi Katafuchi, et al. Differential specificity of human and Escherichia coli endonuclease III and VIII homologues for oxidative base lesions. J Biol Chem. 2004 Apr 2;279(14):14464-71. [Content Brief]

[12]. X Liu, et al. Mutation at active site lysine 212 to arginine uncouples the glycosylase activity from the lyase activity of human endonuclease III. Biochemistry. 2001 Nov 13;40(45):13617-22. [Content Brief]

[13]. T Bessho, et al. Nucleotide excision repair 3' endonuclease XPG stimulates the activity of base excision repairenzyme thymine glycol DNA glycosylase. Nucleic Acids Res. 1999 Feb 15;27(4):979-83. [Content Brief]

[14]. Ian D Odell, et al. Non-specific DNA binding interferes with the efficient excision of oxidative lesions from chromatin by the human DNA glycosylase, NEIL1. DNA Repair (Amst). 2010 Feb 4;9(2):134-43. [Content Brief]

[15]. Qiu-Mei Zhang, et al. DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of the hNEIL1 and hNTH1 enzymes in human cells. DNA Repair (Amst). 2005 Jan 2;4(1):71-9. [Content Brief]

[16]. Y Matsumoto, et al. Escherichia coli Nth and human hNTH1 DNA glycosylases are involved in removal of 8-oxoguanine from 8-oxoguanine/guanine mispairs in DNA. Nucleic Acids Res. 2001 May 1;29(9):1975-81. [Content Brief]

[17]. L Luna, et al. Cell-cycle regulation, intracellular sorting and induced overexpression of the human NTH1 DNA glycosylase involved in removal of formamidopyrimidine residues from DNA. Mutat Res. 2000 Jul 25;460(2):95-104. [Content Brief]

[18]. S Ikeda, et al. Purification and characterization of human NTH1, a homolog of Escherichia coli endonuclease III. Direct identification of Lys-212 as the active nucleophilic residue. J Biol Chem. 1998 Aug 21;273(34):21585-93. [Content Brief]

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