Utilization of a Synthetic Peptide as a Tool to Study the Interaction of Heavy Metals with the Zinc Finger Domain of Proteins Critical for Gene Expression in the Developing Brain

Razmiafshari, Morad; Zawia, Nasser H.

doi:10.1006/taap.2000.8950

Cited by 41 publications

(43 citation statements)

References 27 publications

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“…species where zinc(II) is also bound to the ligand besides cadmium(II). Although no specific structures for such species can be proposed 16 from our data, mixed binding of zinc(II) and other metal ions (including cadmium(II) and mercury(II)) to certain zinc finger sites has already been suggested [65,69,71,72].…”

Section: Competition Of Zinc(ii) With Cadmium(ii) or Mercury(ii) In Bmentioning

confidence: 64%

Competition of zinc(II) with cadmium(II) or mercury(II) in binding to a 12-mer peptide

Jancsó

Gyurcsik

Mesterházy

et al. 2013

Journal of Inorganic Biochemistry

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Section: Competition Of Zinc(ii) With Cadmium(ii) or Mercury(ii) In Bmentioning

confidence: 64%

Competition of zinc(II) with cadmium(II) or mercury(II) in binding to a 12-mer peptide

Jancsó

Gyurcsik

Mesterházy

et al. 2013

Journal of Inorganic Biochemistry

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“…Cd may prevent the binding of the MTase Zn finger to DNA. Such effects by Cd have been shown with other Zn finger proteins (11,15). The Zn finger domain in mammalian MTase is not essential for catalytic activity, but its absence alters site specificity and increases the de novo methylation activity of the enzyme (16).…”

Section: Metals Toxicity • Poirier and Vlasovamentioning

confidence: 82%

The prospective role of abnormal methyl metabolism in cadmium toxicity.

Poirier

Власова²

2002

Environ Health Perspect

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Several lines of evidence point to the probable role of abnormal methylation processes in the toxicology of metals and other xenobiotics. The spectrum of toxic effects exhibited by such metals as Ni, As, and Cd, as well as by Zn deficiency, often resemble those seen in animals chronically fed methyl-deficient diets. These metal-associated pathologies include cancer, atherosclerosis, birth defects, neurological disturbances, and pancreatic lesions. In addition, each of the above agents has been shown to alter normal methyl group metabolism in vivo or in vitro. In the present studies, we compared the effects on the enzyme DNA methyltransferase (MTase) of two metal ions: the essential metal Zn and the carcinogen Cd. MTase extracts were obtained from the hepatic nuclei of rats fed a methyl-deficient diet (lacking choline and folate) for 7 and 24 weeks. Control animals were fed the same diet supplemented with each of these vitamins. Zn and Cd both inhibited MTase in the nuclear extracts from both the control and the methyl-deficient rats. The inhibitory activity of Cd was greater than that of Zn regardless of whether the nuclear extracts were from the control or the deficient animals. In addition, the kinetics of Cd inhibition of MTase activity were different in the nuclear extracts from the control and methyl-deficient rats. The results provide evidence that the carcinogenic effects of Cd may be mediated in part through abnormal DNA methylation. Key words: Cd, Zn, carcinogenesis, DNA methyltransferase, methyl deficiency.

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“…4, for example. A second paper offered spectrophotometric data to support metal-thiolate complexation had occurred and displayed gels of electrophoretic mobility shift assays that were interpreted as demonstrating the various metallo-fingers bind to an Sp1 cognate DNA oligomer [55]. Neither is convincing: In particular, the electrophoresis experiments did not reveal the typical retardation in mobility of the metallopeptide-DNA adduct that is characteristic of specific protein-DNA binding (Figs.…”

Section: Discussionmentioning

confidence: 99%

Zn-, Cd-, and Pb-transcription factor IIIA: properties, DNA binding, and comparison with TFIIIA-finger 3 metal complexes

Huang

Krepkiy

et al. 2004

Journal of Inorganic Biochemistry

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Properties of the metal ion binding sites of Zn-transcription factor IIIA (TFIIIA) were investigated to understand the potential of this type of zinc finger to undergo reactions that remove Zn 2+ from the protein. Zn-TFIIIA was purified from E. coli containing the cloned sequence for Xenopus laevis oocyte TFIIIA and its stoichiometry of bound Zn 2+ was shown to depend on the details of the isolation process. The average dissociation constant of Zn 2+ in Zn-TFIIIIA was 10 −7 . The dissociation constant for Zn-F3, the third finger from the N-terminus of TFIIIA, was 1.0 × 10 −8 . The reactivity of Zn-TFIIIA with a series of metal binding ligands, including 2-carboxy-2′-hydroxy-5′-sulfoformazylbenzene (zincon), 4-(2-pyridylazo)-resorcinol (PAR), and 3-ethoxy-2-oxo-butyraldehyde-bis-(N 4 -dimethylthiosemicarbazone) (H 2 KTSM 2 ) revealed similar kinetics. The reactivity of PAR with Zn-TFIIIA declined substantially when the protein was bound to the internal control region (ICR) of the 5S ribosomal DNA. Both Cd 2+ and Pb 2+ disrupt TFIIIA binding to its cognate DNA sequence. The Pb 2+ dissociation constant of Pb-F3 was measured as 2.5 × 10 −8 . According to NMR spectroscopy, F3 does not fold into a regular conformation in the presence of Pb 2+ .

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Utilization of a Synthetic Peptide as a Tool to Study the Interaction of Heavy Metals with the Zinc Finger Domain of Proteins Critical for Gene Expression in the Developing Brain

Cited by 41 publications

References 27 publications

Competition of zinc(II) with cadmium(II) or mercury(II) in binding to a 12-mer peptide

Competition of zinc(II) with cadmium(II) or mercury(II) in binding to a 12-mer peptide

The prospective role of abnormal methyl metabolism in cadmium toxicity.

Zn-, Cd-, and Pb-transcription factor IIIA: properties, DNA binding, and comparison with TFIIIA-finger 3 metal complexes

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