Binding of mismatch repair protein MutS to mispaired DNA adducts of intercalating ruthenium(II) arene complexes
Jazyk angličtina Země Německo Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
- MeSH
- adukty DNA chemie účinky léků MeSH
- anthraceny chemie MeSH
- chybné párování bází * účinky léků MeSH
- cymeny MeSH
- DNA chemie účinky léků MeSH
- Escherichia coli chemie MeSH
- ethylendiaminy chemie MeSH
- interkalátory chemie farmakologie MeSH
- molekulární struktura MeSH
- monoterpeny chemie MeSH
- organokovové sloučeniny chemie farmakologie MeSH
- poškození DNA MeSH
- ruthenium chemie MeSH
- sekvence nukleotidů MeSH
- vazba proteinů MeSH
- vazebná místa MeSH
- vazebný protein MutS opravné syntézy DNA chemie účinky léků MeSH
- vztahy mezi strukturou a aktivitou MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- 4-cymene MeSH Prohlížeč
- adukty DNA MeSH
- anthraceny MeSH
- cymeny MeSH
- DNA MeSH
- ethylendiaminy MeSH
- ethylenediamine MeSH Prohlížeč
- interkalátory MeSH
- monoterpeny MeSH
- organokovové sloučeniny MeSH
- ruthenium MeSH
- vazebný protein MutS opravné syntézy DNA MeSH
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.
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