Mismatch dependent uracil-thymine-DNA glycosylases excise exocyclic hydroxyethano and hydroxypropano cytosine adducts

• Autorzy: Borys-Brzywczy E. , Arczewska K.D. , Saparbaev M. , Hardeland U. , Schar P. , Kusmierek J.T.
• Języki publikacji: EN

Abstrakty

EN

Exocyclic adducts of DNA bases, such as etheno- and hydroxyalkano- ones, are generated by a variety of bifunctional agents, including endogenously formed products of lipid peroxidation. In this work we selectively modified cytosines in the 5’-d(TTT TTT CTT TTT CTT TTT CTT TTT T)-3’ oligonucleotide using: chloroacetaldehyde to obtain 3,N4-α-hydroxyethano- (HEC) and 3,N4-etheno- (epsilonC), acrolein to obtain 3,N4-α-hydroxypropano- (HPC) and crotonaldehyde to obtain 3,N4αhydroxy-γ-methylpropano- (mHPC) adducts of cytosine. The studied adducts are alkali-labile which results in oligonucleotide strain breaks at the sites of modification upon strong base treatment. The oligonucleotides carrying adducted cytosines were studied as substrates of Escherichia coli Mug, human TDG and fission yeast Thp1p glycosylases. All the adducts studied are excised by bacterial Mug although with various efficiency: εC > HEC > HPC > mHPC. The yeast enzyme excises efficiently εC≥HEC>HPC, whereas the human enzyme excises only εC. The pH-dependence curves of excision of εC, HEC and HPC by Mug are bell shaped and the most efficient excision of adducts occurs within the pH range of 8.6–9.6. The observed increase of excision of HEC and HPC above pH 7.2 can be explained by deprotonation of these adducts, which are high pKa compounds and exist in a protonated form at neutrality. On the other hand, since εC is in a neutral form in the pH range studied, we postulate an involvement of an additional catalytic factor. We hypothesize that the enzyme structure undergoes a pH-induced rearrangement allowing the participation of Lys68 of Mug in catalysis via a hydrogen bond interaction of its ε-amino group with N4 of the cytosine exocyclic adducts.

Słowa kluczowe

EN

3-methyladenine DNA glycosylase; chloroacetaldehyde; mismatch uracil-DNA glycosylase; trans-4-hydroxy-2-nonenal; uracil-DNA glycosylase; lipid peroxidation; exocyclic DNA base adduct; cytosine adduct; Thp1p glycosylase; thymine glycol glycosylase; man; mismatch thymine-DNA glycosylase; base excision repair; exocyclic cytosine adduct; acrolein; Escherichia coli; crotonaldehyde; thymine-DNA glycosylase; N-alkylpurine-DNA glycosylase

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2005
• Tom: 52
• Numer: 1
• Opis fizyczny: p.149-165,fig.,ref.

Twórcy

autor

Borys-Brzywczy E.

• Polish Academy of Sciences, A.Pawinskiego 5A, 02-106 Warsaw, Poland

autor

Arczewska K.D.

autor

Saparbaev M.

autor

Hardeland U.

autor

Schar P.

autor

Kusmierek J.T.

Bibliografia

• Barrett TE, Savva R, Panayotou G, Barlow T, Brown T, Jiricny J, Pearl LH. (1998) Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary- strand interactions. Cell.; 92: 117–29.
• Barrett TE, Schärer OD, Savva R, Brown T, Jiricny J, Verdine GL, Pearl LH. (1999) Crystal structure of a thwarted mismatch glycosylase DNA repair complex. EMBO J.; 18: 6599–609.
• Barrio RJ, Secrist JA, Leonard NJ. (1972) Fluorescent adenosine and cytidine derivatives. Biochem Biophys Res Commun.; 46: 597–604.
• Bartsch H. (1999) Keynote address: Exocyclic adducts as new risk markers for DNA damage in man. In Exocyclic DNA Adducts in Mutagenesis and Carcinogenesis. Singer B, Bartsch H, eds, pp 1–16. IARC Scientific Publication No. 150, IARC, Lyon.
• Berens K, Shugar D. (1963) Ultraviolet absorption spectra and structure of halogenated uracils and their glycosides. Acta Biochim Polon.; 10: 25–48.
• Borys E, Kuśmierek JT. (1998) Endogenous and exogenous DNA lesions recognised by N-alkylpurine-DNA glycosylases. Acta Biochim Polon.; 45: 579–86.
• Chenna A, Iden CR. (1993) Characterization of 2-deoxycytidine and 2-deoxyuridine adducts formed in reactions with acrolein and 2-bromoacrolein. Chem Res Toxicol.; 6: 261–8.
• Chenna A, Rieger RA, Iden CR. (1992) Characterization of thymidine adducts formed by acrolein and 2-bromoacrolein. Carcinogenesis.; 13: 2361–5.
• Chung FL, Zhang L, Ocando JE, Nath RG. (1999) Role of 1,N2-propanodeoxyguanosine adducts as endogenous DNA lesions in rodents and humans. In Exocyclic DNA Adducts in Mutagenesis and Carcinogenesis. Singer B, Bartsch H, eds, pp 45–54. IARC Scientific Publication No. 150, IARC, Lyon.
• Curren RD, Yang LL, Conklin PM, Grafstrom RC, Harris CC. (1988) Mutagenesis of xeroderma pigmentosum fibroblasts by acrolein. Mutat Res.; 209: 17–22.
• Hang B, Medina M, Fraenkel-Conrat H, Singer B. (1998) A 55-kDa protein isolated from human cells shows DNA glycosylase activity toward 3,N4-ethenocytosine and the G/T mismatch. Proc Natl Acad Sci USA.; 95: 13561–6.
• Hang B, Downing G, Guliaev AB, Singer B. (2002) Novel activity of Escherichia coli mismatch uracil-DNA glycosylase (Mug) excising 8-(hydroxymethyl)-3,N4-ethenocytosine, a potential product resulting from glycilaldehyde reaction. Biochemistry.; 41: 2158–65.
• Hardeland U, Bentle M, Jiricny J, Schär P. (2000) Separating substrate recognition from base hydrolysis in human thymine DNA glycosylase by mutational analysis. J Biol Chem.; 275: 33449–56.
• Hardeland U, Bentle M, Jiricny J, Schär P. (2003) The versatile thymine DNA-glycosylase: a comparative characterization of the human, Drosophila and fission yeast orthologs. Nucleic Acids Res.; 31: 2261–71.
• Kowalczyk P, Cieśla JM, Komisarski M, Kuśmierek JT, Tudek B. (2004) Long-chain adducts of trans-4-hydroxy-2-nonenal to DNA bases cause recombination, base substitutions and frameshift mutations in M13 phage. Mutat Res.; 550: 33–48.
• Krokan HE, Drablos F, Slupphaug G. (2002) Uracil in DNA — occurence, consequences and repair. Oncogene.; 21: 8935–48.
• Krzyżosiak WJ, Biernat J, Ciesiołka J, Górnicki P, Wiewiórowski M. (1979) Further studies on adenosine and cytidine reaction with chloroacetaldehyde, a new support for the cyclic carbinolamine structure of the stable reaction intermediate and its relevance to the reaction mechanism and tRNA modification. Polish J Chem.; 53: 243–52.
• Kuśmierek JT, Singer B. (1982) Chloroacetaldehyde- treated ribo- and deoxyribopolynucleotides. 1. Reaction products. Biochemistry.; 21: 5717–22.
• Leonard NJ. (1984) Etheno-substituted nucleotides and coenzymes: fluorescence and biological activity. CRC Crit Rev Biochem.; 15: 125–99.
• Lindahl T. (1993) Instability and decay of the primary structure of DNA. Nature.; 362: 709–15.
• Liu P, Burdzy A, Sowers LC. (2002) Substrate recognition by a family of uracil-DNA glycosylases: UNG, MUG, and TDG. Chem Res Toxicol.; 15: 1001–9.
• Marnett LJ, Hurd HK, Hollstein MC, Levin DE, Esterbauer H, Ames BN. (1985) Naturally occurring carbonyl compounds are mutagens in Salmonella tester strain TA104. Mutat Res.; 148: 25–34.
• Matijasevic Z, Sekiguchi M, Ludlum D. (1992) Release of N2,3-ethenoguanine from chloroacetaldehyde-treated DNA by Escherichia coli 3-methyladenie DNA glycosylase II. Proc Natl Acad Sci USA.; 89: 9331–4.
• Oivanen M, Hovinen J, Lehikoinen P, Lönnberg H. (1993) Hydrolysis of N-glycosidic bond of nucleosides and nucleotides. Trends Organ Chem.; 4: 397–412.
• O’Neill RJ, Vorob’eva OV, Shahbakhti H, Zmuda E, Bhagwat AS, Baldwin GS. (2003) Mismatch uracil glycosylase from Escherichia coli. A general mismatch or a specific DNA glycosylase? J Biol Chem.; 278: 20526–32.
• Pearl LH. (2000) Structure and function in the uracil-DNA glycosylase superfamily. Mutat Res.; 460: 165–81.
• Saparbaev M, Laval J. (1998) 3,N4-ethenocytosine, a highly mutagenic adduct, is a primary substrate for Escherichia coli double- stranded uracil-DNA glycosylase and human mismatch-specific thymine-DNAglycosylase. Proc Natl Acad Sci USA.; 95: 8508–13.
• Saparbaev M, Kleibl K, Laval J. (1995) Escherichia coli, Saccharomyces cerevisiae, rat and human 3-methyladenine DNA glycosylases repair 1,N6-ethenoadenine when present in DNA. Nucleic Acids Res.; 23: 3750–75.
• Saparbaev MK, Langouet S, Privezentzev CV, Guengerich FP, Cai H, Elder RH, Laval J. (2002) 1,N2-ethenoguanine, a mutagenic DNA adduct, is a substrate of Escherichia coli mismatch-specific uracil-DNA glycosylase and human alkylpurine-DNA-N-glycosylase. J Biol Chem.; 277: 26987–93.
• Savva R, McAuley-Hecht K, Brown T, Pearl L. (1995) The structural basis of specific base-excision repair by uracil-DNA glycosylase. Nature.; 373: 487–93.
• Secrist JA, Barrio JR, Leonard NJ, Weber G. (1972) Fluorescent modification of adenosine-containing coenzymes. Biological activities and spectroscopic properties. Biochemistry.; 11: 3499–506.
• Shapiro R, Danzig M. (1972) Acidic hydrolysis of deoxycytidine and deoxyuridine derivatives. The general mechanism of deoxyribonucleoside hydrolysis. Biochemistry.; 11: 23–9.
• Sierzputowska-Gracz H, Wiewiórowski M, Kozerski L, von Philipsborn W. (1984) Proton coupled 15N NMR spectra of neutral and protonated ethenoadenosine and ethenocytidine. Nucleic Acids Res.; 12: 6247–58.
• Singer B, Antoccia A, Basu AK, Dosanjh MK, Fraenkel-Conrat H, Gallagher PE, Kuśmierek JT, Qiu ZH, Rydberg B. (1992) Both purified human 1,N6-ethenoadenine-binding protein and purified human 3-methyladenine-DNA glycosylase act on 1,N6-ethenoadenine and 3-methyladenine. Proc Natl Acad Sci USA.; 89: 9386–90.
• Smith RA, Williamson DS, Cerny RL, Cohen SM. (1990) Detection of 1,N6-propanodeoxyadenosine in acrolein-modified polydeoxyadenylic acid and in DNA by 32P postlabeling. Cancer Res.; 50: 3005–12.
• Speina E, Cieśla JM, Wójcik J, Bajek M, Kuśmierek JT, Tudek B. (2001) The pyrimidine ring-opened derivative of 1,N6-ethenoadenine is excised from DNA by the Escherichia coli Fpg and Nth proteins. J Biol Chem.; 276: 21821–7.
• Tudek B, VanZeeland AA, Kuśmierek JT, Laval J. (1998) Activity of Escherichia coli
• DNA-glycosylases on DNA damaged by methylating and ethylating agents and influence of 3-substituted adenine derivatives. Mutat Res.; 407: 169–76.
• Yang IY, Hossain M, Miller H, Khullar S, Johnson F, Grollman A, Moriya M. (2001) Responses to the major acrolein-derived deoxyguanosine adduct in Escherichia coli. J Biol Chem.; 276: 9071–96.