Detailed Information on Publication Record
2008
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 et. al.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
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10610 Biophysics
Country of publisher
Germany
Confidentiality degree
není předmětem státního či obchodního tajemství
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
Tags
International impact, Reviewed
Změněno: 25/6/2009 12:30, Mgr. María Victoria Marini Palomeque, Ph.D.
V originále
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.
In Czech
Cíl práce byl studovat afinitu proteinu MutS na poškozenou DNA.
Links
LC06030, research and development project |
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