J 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; Hana KOSTRHUNOVA; María Victoria MARINI PALOMEQUE; Jana KAŠPÁRKOVÁ; Peter J. SADLER; Jean-Marc MALINGE and Viktor BRABEC

Edition

Journal of Biological Inorganic Chemistry, Germany, Springer Berlin / Heidelberg, 2008, 0949-8257

Other information

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

Marked to be transferred to RIV

Yes

RIV identification code

RIV/00216224:14310/08:00035834

Organization unit

Faculty of Science

UT WoS

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

Abstract

ORIG CZ

In the original language

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