CASTELLANO-CASTILLO, Maria, Hana KOSTRHUNOVA, María Victoria MARINI PALOMEQUE, Jana KAŠPÁRKOVÁ, Peter J. SADLER, Jean-Marc MALINGE and Viktor BRABEC. Binding of mismatch repair protein MutS to mispaired DNA adducts of intercalating ruthenium(II) arene complexes. Journal of Biological Inorganic Chemistry. Germany: Springer Berlin / Heidelberg, 2008, vol. 13, No 6, p. 993-999. ISSN 0949-8257. |
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@article{837281, author = {CastellanoandCastillo, Maria and Kostrhunova, Hana and Marini Palomeque, María Victoria and Kašpárková, Jana and Sadler, Peter J. and Malinge, JeanandMarc and Brabec, Viktor}, article_location = {Germany}, article_number = {6}, keywords = {DNA ; Mismatch repair ; MutS ; Ruthenium arene ; Intercalation}, language = {eng}, issn = {0949-8257}, journal = {Journal of Biological Inorganic Chemistry}, title = {Binding of mismatch repair protein MutS to mispaired DNA adducts of intercalating ruthenium(II) arene complexes}, volume = {13}, year = {2008} }
TY - JOUR ID - 837281 AU - Castellano-Castillo, Maria - Kostrhunova, Hana - Marini Palomeque, María Victoria - Kašpárková, Jana - Sadler, Peter J. - Malinge, Jean-Marc - Brabec, Viktor PY - 2008 TI - Binding of mismatch repair protein MutS to mispaired DNA adducts of intercalating ruthenium(II) arene complexes JF - Journal of Biological Inorganic Chemistry VL - 13 IS - 6 SP - 993-999 EP - 993-999 PB - Springer Berlin / Heidelberg SN - 09498257 KW - DNA KW - Mismatch repair KW - MutS KW - Ruthenium arene KW - Intercalation N2 - The present study was performed to examine the affinity of Escherichia coli mismatch repair (MMR) protein MutS for DNA damaged by an intercalating compound. We examined the binding properties of this protein with various DNA substrates containing a single centrally located adduct of ruthenium(II) arene complexes [(eta(6)-arene)Ru(II)(en)Cl][PF(6)] [arene is tetrahydroanthracene (THA) or p-cymene (CYM); en is ethylenediamine]. These two complexes were chosen as representatives of two different classes of monofunctional ruthenium(II) arene compounds which differ in DNA-binding modes: one that involves combined coordination to G N7 along with noncovalent, hydrophobic interactions, such as partial arene intercalation (tricyclic-ring Ru-THA), and the other that binds to DNA only via coordination to G N7 and does not interact with double-helical DNA by intercalation (monoring Ru-CYM). Using electrophoretic mobility shift assays, we examined the binding properties of MutS protein with various DNA duplexes (homoduplexes or mismatched duplexes) containing a single centrally located adduct of ruthenium(II) arene compounds. We have shown that presence of the ruthenium(II) arene adducts decreases the affinity of MutS for ruthenated DNA duplexes that either have a regular sequence or contain a mismatch and that intercalation of the arene contributes considerably to this inhibitory effect. Since MutS initiates MMR by recognizing DNA lesions, the results of the present work support the view that DNA damage due to intercalation is removed from DNA by a mechanism(s) other than MMR. ER -
CASTELLANO-CASTILLO, Maria, Hana KOSTRHUNOVA, María Victoria MARINI PALOMEQUE, Jana KAŠPÁRKOVÁ, Peter J. SADLER, Jean-Marc MALINGE and Viktor BRABEC. Binding of mismatch repair protein MutS to mispaired DNA adducts of intercalating ruthenium(II) arene complexes. \textit{Journal of Biological Inorganic Chemistry}. Germany: Springer Berlin / Heidelberg, 2008, vol.~13, No~6, p.~993-999. ISSN~0949-8257.
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