Binding of mismatch repair protein MutS to mispaired DNA adducts of intercalating ruthenium(II) arene complexes

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.

Basic information

• Original name: Binding of mismatch repair protein MutS to mispaired DNA adducts of intercalating ruthenium(II) arene complexes
• Name in Czech: Vazba MutS na nezparovane DNA adukty interkalujicich rutheniovych komplexu
• Authors: CASTELLANO-CASTILLO, Maria (724 Spain), Hana KOSTRHUNOVA (203 Czech Republic), María Victoria MARINI PALOMEQUE (858 Uruguay), Jana KAŠPÁRKOVÁ (203 Czech Republic), Peter J. SADLER (826 United Kingdom of Great Britain and Northern Ireland), Jean-Marc MALINGE (250 France) and Viktor BRABEC (203 Czech Republic, guarantor).
• Edition: Journal of Biological Inorganic Chemistry, Germany, Springer Berlin / Heidelberg, 2008, 0949-8257.

Other information

• Original language: English
• Type of outcome: Article in a journal
• Field of Study: 10610 Biophysics
• Country of publisher: Germany
• Confidentiality degree: is not subject to a state or trade secret
• Impact factor: Impact factor: 3.600
• RIV identification code: RIV/00216224:14310/08:00035834
• Organization unit: Faculty of Science
• UT WoS: 000257934500014
• Keywords (in Czech): DNA ; Oprava nezparovanych bazi; MutS; rutheniove areny; interkalace
• Keywords in English: DNA ; Mismatch repair ; MutS ; Ruthenium arene ; Intercalation
• Tags: DNA, intercalation, MISMATCH REPAIR, MutS, Ruthenium arene
• Tags: International impact, Reviewed

Abstract

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.

Abstract (in Czech)

Cíl práce byl studovat afinitu proteinu MutS na poškozenou DNA.

Links

• LC06030, research and development project: Name: Biomolekulární centrum

Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular centre