Literature DB >> 12909623

Site-specific DNA transesterification by vaccinia topoisomerase: effects of benzo[alpha]pyrene-dA, 8-oxoguanine, 8-oxoadenine and 2-aminopurine modifications.

Lyudmila Yakovleva1, Ligeng Tian, Jane M Sayer, Govind P Kalena, Heiko Kroth, Donald M Jerina, Stewart Shuman.   

Abstract

Vaccinia DNA topoisomerase forms a covalent DNA-(3'-phosphotyrosyl)-enzyme intermediate at a specific target site 5'-C+5C+4C+3T+2T+1p downward arrow N-1 in duplex DNA. Here we study the effects of base modifications on the rate and extent of single-turnover DNA transesterification. Chiral trans opened C-10 R and S adducts of benzo[a]pyrene (BP) 7,8-diol 9,10-epoxide were introduced at single N6-deoxyadenosine (dA) positions within the 3'-G+5G+4G+3A+2A+1T-1A-2 sequence of the nonscissile DNA strand. The R and S BPdA adducts intercalate from the major groove on the 5' and 3' sides of the modified base, respectively, and perturb local base stacking. We found that R and S BPdA modifications at +1A reduced the transesterification rate by a factor of 700-1000 without affecting the yield of the covalent topoisomerase-DNA complex. BPdA modifications at +2A reduced the extent of transesterification and elicited rate decrements of 200- and 7000-fold for the S and R diastereomers, respectively. In contrast, BPdA adducts at the -2 position had no effect on the extent of the reaction and relatively little impact on the rate of cleavage. A more subtle probe of major groove contacts entailed substituting each of the purines of the nonscissile strand with its 8-oxo analog. The +3 oxoG modification slowed transesterification 35-fold, whereas other 8-oxo modifications were benign. 8-Oxo substitutions at the -1 position in the scissile strand slowed single-turnover cleavage by a factor of six but had an even greater slowing effect on religation, which resulted in an increase in the cleavage equilibrium constant. 2-Aminopurine at positions +3, +4, or +5 in the nonscissile strand had no effect on transesterification per se but had synergistic effects when combined with 8-oxoA at position -1 in the scissile strand. These findings illuminate the functional interface of vaccinia topoisomerase with the DNA major groove.

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Year:  2003        PMID: 12909623     DOI: 10.1074/jbc.M308079200

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  4 in total

1.  Major groove interactions of vaccinia Topo I provide specificity by optimally positioning the covalent phosphotyrosine linkage.

Authors:  Rajesh Nagarajan; James T Stivers
Journal:  Biochemistry       Date:  2006-05-09       Impact factor: 3.162

2.  Chemical and traditional mutagenesis of vaccinia DNA topoisomerase provides insights to cleavage site recognition and transesterification chemistry.

Authors:  Lyudmila Yakovleva; Shengxi Chen; Sidney M Hecht; Stewart Shuman
Journal:  J Biol Chem       Date:  2008-03-25       Impact factor: 5.157

3.  Probing murine methyltransfease Dnmt3a interactions with benzo[a]pyrene-modified DNA by fluorescence methods.

Authors:  Antonio S Minero; Olga V Lukashevich; Natalia A Cherepanova; Alexander Kolbanovskiy; Nicholas E Geacintov; Elizaveta S Gromova
Journal:  FEBS J       Date:  2012-09-11       Impact factor: 5.542

4.  Position- and orientation-specific enhancement of topoisomerase I cleavage complexes by triplex DNA structures.

Authors:  Smitha Antony; Paola B Arimondo; Jian-Sheng Sun; Yves Pommier
Journal:  Nucleic Acids Res       Date:  2004-10-04       Impact factor: 16.971

  4 in total

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