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Binding of mismatch repair protein MutS to mispaired DNA adducts of intercalating ruthenium(II) arene complexes
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Castellano-Castillo, Maria, Kostrhunova, Hana, Marini, Victoria, Kasparkova, Jana, Sadler, P. J., Malinge, Jean-Marc and Brabec, V. (Viktor) (2008) Binding of mismatch repair protein MutS to mispaired DNA adducts of intercalating ruthenium(II) arene complexes. Journal of Biological Inorganic Chemistry, Vol.13 (No.6). pp. 993-999. doi:10.1007/s00775-008-0386-3
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Official URL: http://dx.doi.org/10.1007/s00775-008-0386-3
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][PF6] [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.
| Item Type: | Journal Article | ||||
|---|---|---|---|---|---|
| Subjects: | Q Science > QD Chemistry Q Science > QH Natural history > QH426 Genetics Q Science > QP Physiology |
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| Divisions: | Faculty of Science > Chemistry | ||||
| Library of Congress Subject Headings (LCSH): | Ruthenium compounds, Clathrate compounds, G proteins, DNA repair, DNA damage, Protein binding, DNA-protein interactions | ||||
| Journal or Publication Title: | Journal of Biological Inorganic Chemistry | ||||
| Publisher: | Springer | ||||
| ISSN: | 0949-8257 | ||||
| Official Date: | August 2008 | ||||
| Dates: |
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| Volume: | Vol.13 | ||||
| Number: | No.6 | ||||
| Number of Pages: | 7 | ||||
| Page Range: | pp. 993-999 | ||||
| DOI: | 10.1007/s00775-008-0386-3 | ||||
| Status: | Peer Reviewed | ||||
| Publication Status: | Published | ||||
| Access rights to Published version: | Restricted or Subscription Access | ||||
| Funder: | Czech Republic. Ministerstvo školství, mládeže a tělovýchovy [Czech Republic. Ministry of Education, Youth, and Sport], Akademie věd České republiky [Academy of Sciences of the Czech Republic] (ASCR), Oncosense Ltd., Spain. Ministerio de Educación, Cultura y Deporte [Spain. Ministry of Education, Culture, and Sports] | ||||
| Grant number: | MSMT LC06030 (CRMEYS), 6198959216 (CRMEYS), ME08017 (CRMEYS), OC08003 (CRMEYS), 1QS500040581 (ASCR), KAN200200651 (ASCR), AV0Z50040507 (ASCR), AV0Z50040702 (ASCR), IAA400040803 (ASCR) |
Data sourced from Thomson Reuters' Web of Knowledge
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