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{{Infobox_gene}}
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'''Endonuclease III-like protein 1''' is an [[enzyme]] that in humans is encoded by the ''NTHL1'' [[gene]].<ref name="pmid9045706">{{cite journal | vauthors = Hilbert TP, Chaung W, Boorstein RJ, Cunningham RP, Teebor GW | title = Cloning and expression of the cDNA encoding the human homologue of the DNA repair enzyme, Escherichia coli endonuclease III | journal = J Biol Chem | volume = 272 | issue = 10 | pages = 6733–40 |date=Apr 1997 | pmid = 9045706 | pmc =  | doi =10.1074/jbc.272.10.6733  }}</ref><ref name="pmid8990169">{{cite journal | vauthors = Aspinwall R, Rothwell DG, Roldan-Arjona T, Anselmino C, Ward CJ, Cheadle JP, Sampson JR, Lindahl T, Harris PC, Hickson ID | title = Cloning and characterization of a functional human homolog of Escherichia coli endonuclease III | journal = Proc Natl Acad Sci U S A | volume = 94 | issue = 1 | pages = 109–14 |date=Feb 1997 | pmid = 8990169 | pmc = 19249 | doi =10.1073/pnas.94.1.109  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: NTHL1 nth endonuclease III-like 1 (E. coli)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4913| accessdate = }}</ref>
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As reviewed by Li et al.,<ref name=Li>{{cite journal |vauthors=Li J, Braganza A, Sobol RW |title=Base excision repair facilitates a functional relationship between Guanine oxidation and histone demethylation |journal=Antioxid. Redox Signal. |volume=18 |issue=18 |pages=2429–43 |year=2013 |pmid=23311711 |pmc=3671628 |doi=10.1089/ars.2012.5107 |url=}}</ref>  NTHL1 is a bifunctional DNA glycosylase that has an associated [[DNA-(apurinic or apyrimidinic site) lyase#Biological Function|beta-elimination]] activity.  NTHL1 is usually involved in removing oxidative pyrimidine lesions through [[base excision repair]].  NTHL1 catalyses the first step in base excision repair.  It cleaves the N-glycosylic bond between the damaged base and its associated sugar residue and then cleaves the phosphodiester bond 3' to the AP site,<ref name="pmid21930793">{{cite journal |vauthors=Odell ID, Barbour JE, Murphy DL, Della-Maria JA, Sweasy JB, Tomkinson AE, Wallace SS, Pederson DS |title=Nucleosome disruption by DNA ligase III-XRCC1 promotes efficient base excision repair |journal=Mol. Cell. Biol. |volume=31 |issue=22 |pages=4623–32 |year=2011 |pmid=21930793 |pmc=3209256 |doi=10.1128/MCB.05715-11 |url=}}</ref> leaving a 3'-unsaturated aldehyde after beta-elimination and a 5'-phosphate at the termini of the repair gap.<ref name=Li />
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Low expression of NTHL1 is associated with initiation and development of astrocytoma.<ref name="pmid17034947">{{cite journal |vauthors=Jiang Z, Hu J, Li X, Jiang Y, Zhou W, Lu D |title=Expression analyses of 27 DNA repair genes in astrocytoma by TaqMan low-density array |journal=Neurosci. Lett. |volume=409 |issue=2 |pages=112–7 |year=2006 |pmid=17034947 |doi=10.1016/j.neulet.2006.09.038 |url=}}</ref> Low expression of NTHL1 is also found in follicular thyroid tumors.<ref name="pmid22331172">{{cite journal |vauthors=Karger S, Krause K, Engelhardt C, Weidinger C, Gimm O, Dralle H, Sheu-Grabellus SY, Schmid KW, Fuhrer D |title=Distinct pattern of oxidative DNA damage and DNA repair in follicular thyroid tumours |journal=J. Mol. Endocrinol. |volume=48 |issue=3 |pages=193–202 |year=2012 |pmid=22331172 |doi=10.1530/JME-11-0119 |url=}}</ref>
{{GNF_Protein_box
| image =
A germ line homozygous mutation in ''NTHL1'' causes a cancer susceptibility syndrome similar to [[Hereditary nonpolyposis colorectal cancer|Lynch syndrome]].<ref name="pmid26431160">{{cite journal |vauthors=Kuiper RP, Hoogerbrugge N |title=NTHL1 defines novel cancer syndrome |journal=Oncotarget |volume= 6|issue= 33|pages= 34069–70|year=2015 |pmid=26431160 |doi= 10.18632/oncotarget.5864|pmc=4741436}}</ref><ref name="pmid25938944">{{cite journal |vauthors=Weren RD, Ligtenberg MJ, Kets CM, de Voer RM, Verwiel ET, Spruijt L, van Zelst-Stams WA, Jongmans MC, Gilissen C, Hehir-Kwa JY, Hoischen A, Shendure J, Boyle EA, Kamping EJ, Nagtegaal ID, Tops BB, Nagengast FM, Geurts van Kessel A, van Krieken JH, Kuiper RP, Hoogerbrugge N |title=A germline homozygous mutation in the base-excision repair gene NTHL1 causes adenomatous polyposis and colorectal cancer |journal=Nat. Genet. |volume=47 |issue=6 |pages=668–71 |year=2015 |pmid=25938944 |doi=10.1038/ng.3287 |url=}}</ref>
| image_source =
| PDB =  
| Name = Nth endonuclease III-like 1 (E. coli)
| HGNCid = 8028
| Symbol = NTHL1
| AltSymbols =; NTH1; OCTS3
| OMIM = 602656
| ECnumber =
| Homologene = 1897
| MGIid = 1313275
  | GeneAtlas_image1 = PBB_GE_NTHL1_209731_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003906 |text = DNA-(apurinic or apyrimidinic site) lyase activity}} {{GNF_GO|id=GO:0004519 |text = endonuclease activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0016798 |text = hydrolase activity, acting on glycosyl bonds}} {{GNF_GO|id=GO:0016829 |text = lyase activity}} {{GNF_GO|id=GO:0019104 |text = DNA N-glycosylase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0051539 |text = 4 iron, 4 sulfur cluster binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}}
| Process = {{GNF_GO|id=GO:0006284 |text = base-excision repair}} {{GNF_GO|id=GO:0006296 |text = nucleotide-excision repair, DNA incision, 5'-to lesion}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4913
    | Hs_Ensembl = ENSG00000065057
    | Hs_RefseqProtein = NP_002519
    | Hs_RefseqmRNA = NM_002528
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 16
    | Hs_GenLoc_start = 2029817
    | Hs_GenLoc_end = 2037868
    | Hs_Uniprot = P78549
    | Mm_EntrezGene = 18207
    | Mm_Ensembl = ENSMUSG00000041429
    | Mm_RefseqmRNA = NM_008743
    | Mm_RefseqProtein = NP_032769
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 17
    | Mm_GenLoc_start = 24360310
    | Mm_GenLoc_end = 24366437
    | Mm_Uniprot = O35980
  }}
}}
'''Nth endonuclease III-like 1 (E. coli)''', also known as '''NTHL1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NTHL1 nth endonuclease III-like 1 (E. coli)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4913| accessdate = }}</ref>


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==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal | author=Hilbert TP, Boorstein RJ, Kung HC, ''et al.'' |title=Purification of a mammalian homologue of Escherichia coli endonuclease III: identification of a bovine pyrimidine hydrate-thymine glycol DNAse/AP lyase by irreversible cross linking to a thymine glycol-containing oligoxynucleotide. |journal=Biochemistry |volume=35 |issue= 8 |pages= 2505-11 |year= 1996 |pmid= 8611553 |doi= 10.1021/bi952516e }}
*{{cite journal   |vauthors=Hilbert TP, Boorstein RJ, Kung HC, etal |title=Purification of a mammalian homologue of Escherichia coli endonuclease III: identification of a bovine pyrimidine hydrate-thymine glycol DNAse/AP lyase by irreversible cross linking to a thymine glycol-containing oligoxynucleotide. |journal=Biochemistry |volume=35 |issue= 8 |pages= 2505–11 |year= 1996 |pmid= 8611553 |doi= 10.1021/bi952516e }}
*{{cite journal | author=Aspinwall R, Rothwell DG, Roldan-Arjona T, ''et al.'' |title=Cloning and characterization of a functional human homolog of Escherichia coli endonuclease III. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 1 |pages= 109-14 |year= 1997 |pmid= 8990169 |doi=  }}
*{{cite journal   |vauthors=Ikeda S, Biswas T, Roy R, etal |title=Purification and characterization of human NTH1, a homolog of Escherichia coli endonuclease III. Direct identification of Lys-212 as the active nucleophilic residue. |journal=J. Biol. Chem. |volume=273 |issue= 34 |pages= 21585–93 |year= 1998 |pmid= 9705289 |doi=10.1074/jbc.273.34.21585 }}
*{{cite journal | author=Hilbert TP, Chaung W, Boorstein RJ, ''et al.'' |title=Cloning and expression of the cDNA encoding the human homologue of the DNA repair enzyme, Escherichia coli endonuclease III. |journal=J. Biol. Chem. |volume=272 |issue= 10 |pages= 6733-40 |year= 1997 |pmid= 9045706 |doi= }}
*{{cite journal   |vauthors=Sarker AH, Ikeda S, Nakano H, etal |title=Cloning and characterization of a mouse homologue (mNthl1) of Escherichia coli endonuclease III. |journal=J. Mol. Biol. |volume=282 |issue= 4 |pages= 761–74 |year= 1999 |pmid= 9743625 |doi= 10.1006/jmbi.1998.2042 }}
*{{cite journal | author=Ikeda S, Biswas T, Roy R, ''et al.'' |title=Purification and characterization of human NTH1, a homolog of Escherichia coli endonuclease III. Direct identification of Lys-212 as the active nucleophilic residue. |journal=J. Biol. Chem. |volume=273 |issue= 34 |pages= 21585-93 |year= 1998 |pmid= 9705289 |doi=  }}
*{{cite journal   |vauthors=Imai K, Sarker AH, Akiyama K, etal |title=Genomic structure and sequence of a human homologue (NTHL1/NTH1) of Escherichia coli endonuclease III with those of the adjacent parts of TSC2 and SLC9A3R2 genes. |journal=Gene |volume=222 |issue= 2 |pages= 287–95 |year= 1999 |pmid= 9831664 |doi=10.1016/S0378-1119(98)00485-5 }}
*{{cite journal  | author=Sarker AH, Ikeda S, Nakano H, ''et al.'' |title=Cloning and characterization of a mouse homologue (mNthl1) of Escherichia coli endonuclease III. |journal=J. Mol. Biol. |volume=282 |issue= 4 |pages= 761-74 |year= 1999 |pmid= 9743625 |doi= 10.1006/jmbi.1998.2042 }}
*{{cite journal  | author=Bessho T |title=Nucleotide excision repair 3' endonuclease XPG stimulates the activity of base excision repairenzyme thymine glycol DNA glycosylase. |journal=Nucleic Acids Res. |volume=27 |issue= 4 |pages= 979–83 |year= 1999 |pmid= 9927729 |doi=10.1093/nar/27.4.979  | pmc=148276  }}
*{{cite journal | author=Imai K, Sarker AH, Akiyama K, ''et al.'' |title=Genomic structure and sequence of a human homologue (NTHL1/NTH1) of Escherichia coli endonuclease III with those of the adjacent parts of TSC2 and SLC9A3R2 genes. |journal=Gene |volume=222 |issue= 2 |pages= 287-95 |year= 1999 |pmid= 9831664 |doi=  }}
*{{cite journal   |vauthors=Luna L, Bjørås M, Hoff E, etal |title=Cell-cycle regulation, intracellular sorting and induced overexpression of the human NTH1 DNA glycosylase involved in removal of formamidopyrimidine residues from DNA. |journal=Mutat. Res. |volume=460 |issue= 2 |pages= 95–104 |year= 2000 |pmid= 10882850 |doi=  10.1016/s0921-8777(00)00015-x}}
*{{cite journal | author=Bessho T |title=Nucleotide excision repair 3' endonuclease XPG stimulates the activity of base excision repairenzyme thymine glycol DNA glycosylase. |journal=Nucleic Acids Res. |volume=27 |issue= 4 |pages= 979-83 |year= 1999 |pmid= 9927729 |doi=  }}
*{{cite journal   |vauthors=Matsumoto Y, Zhang QM, Takao M, etal |title=Escherichia coli Nth and human hNTH1 DNA glycosylases are involved in removal of 8-oxoguanine from 8-oxoguanine/guanine mispairs in DNA. |journal=Nucleic Acids Res. |volume=29 |issue= 9 |pages= 1975–81 |year= 2002 |pmid= 11328882 |doi=10.1093/nar/29.9.1975  | pmc=37258 }}
*{{cite journal | author=Luna L, Bjørås M, Hoff E, ''et al.'' |title=Cell-cycle regulation, intracellular sorting and induced overexpression of the human NTH1 DNA glycosylase involved in removal of formamidopyrimidine residues from DNA. |journal=Mutat. Res. |volume=460 |issue= 2 |pages= 95-104 |year= 2000 |pmid= 10882850 |doi=  }}
*{{cite journal   |vauthors=Miyabe I, Zhang QM, Kino K, etal |title=Identification of 5-formyluracil DNA glycosylase activity of human hNTH1 protein. |journal=Nucleic Acids Res. |volume=30 |issue= 15 |pages= 3443–8 |year= 2002 |pmid= 12140329 |doi=10.1093/nar/gkf460  | pmc=137084 }}
*{{cite journal  | author=Matsumoto Y, Zhang QM, Takao M, ''et al.'' |title=Escherichia coli Nth and human hNTH1 DNA glycosylases are involved in removal of 8-oxoguanine from 8-oxoguanine/guanine mispairs in DNA. |journal=Nucleic Acids Res. |volume=29 |issue= 9 |pages= 1975-81 |year= 2002 |pmid= 11328882 |doi=  }}
*{{cite journal  | vauthors=Liu X, Roy R |title=Truncation of amino-terminal tail stimulates activity of human endonuclease III (hNTH1). |journal=J. Mol. Biol. |volume=321 |issue= 2 |pages= 265–76 |year= 2002 |pmid= 12144783 |doi=10.1016/S0022-2836(02)00623-X }}
*{{cite journal | author=Miyabe I, Zhang QM, Kino K, ''et al.'' |title=Identification of 5-formyluracil DNA glycosylase activity of human hNTH1 protein. |journal=Nucleic Acids Res. |volume=30 |issue= 15 |pages= 3443-8 |year= 2002 |pmid= 12140329 |doi=  }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal | author=Liu X, Roy R |title=Truncation of amino-terminal tail stimulates activity of human endonuclease III (hNTH1). |journal=J. Mol. Biol. |volume=321 |issue= 2 |pages= 265-76 |year= 2002 |pmid= 12144783 |doi= }}
*{{cite journal   |vauthors=Marenstein DR, Chan MK, Altamirano A, etal |title=Substrate specificity of human endonuclease III (hNTH1). Effect of human APE1 on hNTH1 activity. |journal=J. Biol. Chem. |volume=278 |issue= 11 |pages= 9005–12 |year= 2003 |pmid= 12519758 |doi= 10.1074/jbc.M212168200 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | vauthors=Ikeda S, Kohmoto T, Tabata R, Seki Y |title=Differential intracellular localization of the human and mouse endonuclease III homologs and analysis of the sorting signals. |journal=DNA Repair (Amst.) |volume=1 |issue= 10 |pages= 847–54 |year= 2003 |pmid= 12531031 |doi=10.1016/S1568-7864(02)00145-3  }}
*{{cite journal  | author=Marenstein DR, Chan MK, Altamirano A, ''et al.'' |title=Substrate specificity of human endonuclease III (hNTH1). Effect of human APE1 on hNTH1 activity. |journal=J. Biol. Chem. |volume=278 |issue= 11 |pages= 9005-12 |year= 2003 |pmid= 12519758 |doi= 10.1074/jbc.M212168200 }}
*{{cite journal  | vauthors=Liu X, Choudhury S, Roy R |title=In vitro and in vivo dimerization of human endonuclease III stimulates its activity. |journal=J. Biol. Chem. |volume=278 |issue= 50 |pages= 50061–9 |year= 2004 |pmid= 14522981 |doi= 10.1074/jbc.M309997200 }}
*{{cite journal | author=Ikeda S, Kohmoto T, Tabata R, Seki Y |title=Differential intracellular localization of the human and mouse endonuclease III homologs and analysis of the sorting signals. |journal=DNA Repair (Amst.) |volume=1 |issue= 10 |pages= 847-54 |year= 2003 |pmid= 12531031 |doi= }}
*{{cite journal   |vauthors=Katafuchi A, Nakano T, Masaoka A, etal |title=Differential specificity of human and Escherichia coli endonuclease III and VIII homologues for oxidative base lesions. |journal=J. Biol. Chem. |volume=279 |issue= 14 |pages= 14464–71 |year= 2004 |pmid= 14734554 |doi= 10.1074/jbc.M400393200 }}
*{{cite journal | author=Liu X, Choudhury S, Roy R |title=In vitro and in vivo dimerization of human endonuclease III stimulates its activity. |journal=J. Biol. Chem. |volume=278 |issue= 50 |pages= 50061-9 |year= 2004 |pmid= 14522981 |doi= 10.1074/jbc.M309997200 }}
*{{cite journal   |vauthors=Wiederhold L, Leppard JB, Kedar P, etal |title=AP endonuclease-independent DNA base excision repair in human cells. |journal=Mol. Cell |volume=15 |issue= 2 |pages= 209–20 |year= 2004 |pmid= 15260972 |doi= 10.1016/j.molcel.2004.06.003 }}
*{{cite journal | author=Katafuchi A, Nakano T, Masaoka A, ''et al.'' |title=Differential specificity of human and Escherichia coli endonuclease III and VIII homologues for oxidative base lesions. |journal=J. Biol. Chem. |volume=279 |issue= 14 |pages= 14464-71 |year= 2004 |pmid= 14734554 |doi= 10.1074/jbc.M400393200 }}
*{{cite journal   |vauthors=Oyama M, Wakasugi M, Hama T, etal |title=Human NTH1 physically interacts with p53 and proliferating cell nuclear antigen. |journal=Biochem. Biophys. Res. Commun. |volume=321 |issue= 1 |pages= 183–91 |year= 2004 |pmid= 15358233 |doi= 10.1016/j.bbrc.2004.06.136 }}
*{{cite journal | author=Wiederhold L, Leppard JB, Kedar P, ''et al.'' |title=AP endonuclease-independent DNA base excision repair in human cells. |journal=Mol. Cell |volume=15 |issue= 2 |pages= 209-20 |year= 2004 |pmid= 15260972 |doi= 10.1016/j.molcel.2004.06.003 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
*{{cite journal | author=Oyama M, Wakasugi M, Hama T, ''et al.'' |title=Human NTH1 physically interacts with p53 and proliferating cell nuclear antigen. |journal=Biochem. Biophys. Res. Commun. |volume=321 |issue= 1 |pages= 183-91 |year= 2004 |pmid= 15358233 |doi= 10.1016/j.bbrc.2004.06.136 }}
*{{cite journal   |vauthors=Zhang QM, Yonekura S, Takao M, etal |title=DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of the hNEIL1 and hNTH1 enzymes in human cells. |journal=DNA Repair (Amst.) |volume=4 |issue= 1 |pages= 71–9 |year= 2005 |pmid= 15533839 |doi= 10.1016/j.dnarep.2004.08.002 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal | author=Zhang QM, Yonekura S, Takao M, ''et al.'' |title=DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of the hNEIL1 and hNTH1 enzymes in human cells. |journal=DNA Repair (Amst.) |volume=4 |issue= 1 |pages= 71-9 |year= 2005 |pmid= 15533839 |doi= 10.1016/j.dnarep.2004.08.002 }}
}}
}}
{{refend}}
{{refend}}


{{protein-stub}}
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{{gene-16-stub}}

Latest revision as of 13:18, 5 September 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Endonuclease III-like protein 1 is an enzyme that in humans is encoded by the NTHL1 gene.[1][2][3]

As reviewed by Li et al.,[4] NTHL1 is a bifunctional DNA glycosylase that has an associated beta-elimination activity. NTHL1 is usually involved in removing oxidative pyrimidine lesions through base excision repair. NTHL1 catalyses the first step in base excision repair. It cleaves the N-glycosylic bond between the damaged base and its associated sugar residue and then cleaves the phosphodiester bond 3' to the AP site,[5] leaving a 3'-unsaturated aldehyde after beta-elimination and a 5'-phosphate at the termini of the repair gap.[4]

Low expression of NTHL1 is associated with initiation and development of astrocytoma.[6] Low expression of NTHL1 is also found in follicular thyroid tumors.[7]

A germ line homozygous mutation in NTHL1 causes a cancer susceptibility syndrome similar to Lynch syndrome.[8][9]


References

  1. Hilbert TP, Chaung W, Boorstein RJ, Cunningham RP, Teebor GW (Apr 1997). "Cloning and expression of the cDNA encoding the human homologue of the DNA repair enzyme, Escherichia coli endonuclease III". J Biol Chem. 272 (10): 6733–40. doi:10.1074/jbc.272.10.6733. PMID 9045706.
  2. Aspinwall R, Rothwell DG, Roldan-Arjona T, Anselmino C, Ward CJ, Cheadle JP, Sampson JR, Lindahl T, Harris PC, Hickson ID (Feb 1997). "Cloning and characterization of a functional human homolog of Escherichia coli endonuclease III". Proc Natl Acad Sci U S A. 94 (1): 109–14. doi:10.1073/pnas.94.1.109. PMC 19249. PMID 8990169.
  3. "Entrez Gene: NTHL1 nth endonuclease III-like 1 (E. coli)".
  4. 4.0 4.1 Li J, Braganza A, Sobol RW (2013). "Base excision repair facilitates a functional relationship between Guanine oxidation and histone demethylation". Antioxid. Redox Signal. 18 (18): 2429–43. doi:10.1089/ars.2012.5107. PMC 3671628. PMID 23311711.
  5. Odell ID, Barbour JE, Murphy DL, Della-Maria JA, Sweasy JB, Tomkinson AE, Wallace SS, Pederson DS (2011). "Nucleosome disruption by DNA ligase III-XRCC1 promotes efficient base excision repair". Mol. Cell. Biol. 31 (22): 4623–32. doi:10.1128/MCB.05715-11. PMC 3209256. PMID 21930793.
  6. Jiang Z, Hu J, Li X, Jiang Y, Zhou W, Lu D (2006). "Expression analyses of 27 DNA repair genes in astrocytoma by TaqMan low-density array". Neurosci. Lett. 409 (2): 112–7. doi:10.1016/j.neulet.2006.09.038. PMID 17034947.
  7. Karger S, Krause K, Engelhardt C, Weidinger C, Gimm O, Dralle H, Sheu-Grabellus SY, Schmid KW, Fuhrer D (2012). "Distinct pattern of oxidative DNA damage and DNA repair in follicular thyroid tumours". J. Mol. Endocrinol. 48 (3): 193–202. doi:10.1530/JME-11-0119. PMID 22331172.
  8. Kuiper RP, Hoogerbrugge N (2015). "NTHL1 defines novel cancer syndrome". Oncotarget. 6 (33): 34069–70. doi:10.18632/oncotarget.5864. PMC 4741436. PMID 26431160.
  9. Weren RD, Ligtenberg MJ, Kets CM, de Voer RM, Verwiel ET, Spruijt L, van Zelst-Stams WA, Jongmans MC, Gilissen C, Hehir-Kwa JY, Hoischen A, Shendure J, Boyle EA, Kamping EJ, Nagtegaal ID, Tops BB, Nagengast FM, Geurts van Kessel A, van Krieken JH, Kuiper RP, Hoogerbrugge N (2015). "A germline homozygous mutation in the base-excision repair gene NTHL1 causes adenomatous polyposis and colorectal cancer". Nat. Genet. 47 (6): 668–71. doi:10.1038/ng.3287. PMID 25938944.

Further reading