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- Title
Identification of (η<sup>6</sup>-arene)ruthenium(II) protein binding sites in E. coli cells by combined multidimensional liquid chromatography and ESI tandem mass spectrometry: specific binding of [(η<sup>6</sup>- p-cymene)RuCl<sub>2</sub>(DMSO)] to stress-regulated proteins and to helicases
- Authors
Will, Joanna; Kyas, Andreas; Sheldrick, William S.; Wolters, Dirk
- Abstract
An automated multidimensional protein identification technology, which combines biphasic liquid chromatography with electrospray ionisation tandem mass spectrometry (MS/MS), was employed to analyse tryptic peptides from Escherichia coli cells treated with the antiproliferation agent [(η6- p-cymene)RuCl2(DMSO)], where DMSO is dimethyl sulfoxide. MS/MS spectra were recorded for molecular ions generated by neutral loss of p-cymene from intensive peptide ions coordinated by the (η6- p-cymene)RuII fragment. Matching of the MS/MS spectra of the ruthenated peptides to spectra of proteins in the E. coli database enabled the identification of five protein targets for [(η6- p-cymene)RuCl2(DMSO)]. One of these is the constitutive cold-shock protein cspC, which regulates the expression of genes encoding stress-response proteins, and three of the other targets, ppiD, osmY and sucC, are proteins of the latter type. The DNA damage-inducible helicase dinG was likewise established as a protein target. Aspartate carboxylate functions were identified as the probable Ru binding sites in cspC, ppiD and dinG, and threonine and lysine side chains in osmY and sucC, respectively.
- Subjects
ESCHERICHIA coli; PROTEIN binding; RUTHENIUM; LIQUID chromatography; ELECTROSPRAY ionization mass spectrometry; GENE expression
- Publication
Journal of Biological Inorganic Chemistry (JBIC), 2007, Vol 12, Issue 6, p883
- ISSN
0949-8257
- Publication type
Article
- DOI
10.1007/s00775-007-0242-x