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.Základní údaje
Originální název
Binding of mismatch repair protein MutS to mispaired DNA adducts of intercalating ruthenium(II) arene complexes
Název česky
Vazba MutS na nezparovane DNA adukty interkalujicich rutheniovych komplexu
Autoři
CASTELLANO-CASTILLO, Maria (724 Španělsko), Hana KOSTRHUNOVA (203 Česká republika), María Victoria MARINI PALOMEQUE (858 Uruguay), Jana KAŠPÁRKOVÁ (203 Česká republika), Peter J. SADLER (826 Velká Británie a Severní Irsko), Jean-Marc MALINGE (250 Francie) a Viktor BRABEC (203 Česká republika, garant)
Vydání
Journal of Biological Inorganic Chemistry, Germany, Springer Berlin / Heidelberg, 2008, 0949-8257
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
10610 Biophysics
Stát vydavatele
Německo
Utajení
není předmětem státního či obchodního tajemství
Impakt faktor
Impact factor: 3.600
Kód RIV
RIV/00216224:14310/08:00035834
Organizační jednotka
Přírodovědecká fakulta
UT WoS
000257934500014
Klíčová slova česky
DNA ; Oprava nezparovanych bazi; MutS; rutheniove areny; interkalace
Klíčová slova anglicky
DNA ; Mismatch repair ; MutS ; Ruthenium arene ; Intercalation
Štítky
Příznaky
Mezinárodní význam, Recenzováno
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.
Česky
Cíl práce byl studovat afinitu proteinu MutS na poškozenou DNA.
Návaznosti
LC06030, projekt VaV |
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