Zinc To Cadmium Replacement In The Prokaryotic Zinc-Finger Domain (625 views)
Metallomics (ISSN: 1756-591x, 1756-5901, 1756-591xelectronic), 2013 Dec 18; 6(1): 96-104.
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Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 3.978, 5-year impact factor: 4.01
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84890920939&partnerID=40&md5=2cabe7acbff9375f1af7bdac58ff751c
Keywords: Carcinogenic Effects, Cellular Contexts, Dna Binding Activity, Dna Binding Domain, Metal Substitution, Structural Differences, Zinc Finger, Zinc Finger Domains, Cadmium, Proteins, Nitrogen, Zinc Finger Protein, Article, Heteronuclear Single Quantum Coherence, Priority Journal, Protein Dna Binding, Protein Synthesis, Zinc Finger Motif, Agrobacterium Tumefaciens, Amino Acid Sequence, Bacterial Proteins, Binding Sites, Competitive, Dna-Binding Proteins, Magnetic Resonance Spectroscopy, Metalloproteins, Models, Molecular, Molecular Sequence Data, Mutation, Oligonucleotides, Protein Binding, Protein Conformation, Agrobacterium Tumefaciens Genetics Metabolism, Bacterial Proteins Chemistry Genetics Metabolism, Binding Sites Genetics, Cadmium Chemistry, Dna-Binding Proteins Chemistry Genetics Metabolism, Metalloproteins Chemistry Genetics Metabolism, Oligonucleotides Metabolism, Zinc Chemistry,
Affiliations:
*** IBB - CNR ***
Department of Environmental, Biological and Pharmaceutical Sciences and Technologies, Via Vivaldi 43, 81100 Caserta, Italy
Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone 16, 80134 Naples, Italy
Interuniversity Centre for Research on Bioactive Peptides (CIRPEB), University of Naples Federico II, Via Mezzocannone 16, 80134 Naples, Italy
References:
Not available.
Metallomics (ISSN: 1756-591x, 1756-5901, 1756-591xelectronic), 2013 Dec 18; 6(1): 96-104.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 3.978, 5-year impact factor: 4.01
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84890920939&partnerID=40&md5=2cabe7acbff9375f1af7bdac58ff751c
Keywords: Carcinogenic Effects, Cellular Contexts, Dna Binding Activity, Dna Binding Domain, Metal Substitution, Structural Differences, Zinc Finger, Zinc Finger Domains, Cadmium, Proteins, Nitrogen, Zinc Finger Protein, Article, Heteronuclear Single Quantum Coherence, Priority Journal, Protein Dna Binding, Protein Synthesis, Zinc Finger Motif, Agrobacterium Tumefaciens, Amino Acid Sequence, Bacterial Proteins, Binding Sites, Competitive, Dna-Binding Proteins, Magnetic Resonance Spectroscopy, Metalloproteins, Models, Molecular, Molecular Sequence Data, Mutation, Oligonucleotides, Protein Binding, Protein Conformation, Agrobacterium Tumefaciens Genetics Metabolism, Bacterial Proteins Chemistry Genetics Metabolism, Binding Sites Genetics, Cadmium Chemistry, Dna-Binding Proteins Chemistry Genetics Metabolism, Metalloproteins Chemistry Genetics Metabolism, Oligonucleotides Metabolism, Zinc Chemistry,
Affiliations:
*** IBB - CNR ***
Department of Environmental, Biological and Pharmaceutical Sciences and Technologies, Via Vivaldi 43, 81100 Caserta, Italy
Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone 16, 80134 Naples, Italy
Interuniversity Centre for Research on Bioactive Peptides (CIRPEB), University of Naples Federico II, Via Mezzocannone 16, 80134 Naples, Italy
References:
Not available.
Zinc To Cadmium Replacement In The Prokaryotic Zinc-Finger Domain
Given the similar chemical properties of zinc and cadmium, zinc finger domains have been often proposed as mediators of the toxic and carcinogenic effects exerted by this xenobiotic metal. The effects of zinc replacement by cadmium in different eukaryotic zinc fingers have been reported. In the present work, to evaluate the effects of such substitution in the prokaryotic zinc finger, we report a detailed study of its functional and structural consequences on the Ros DNA binding domain (Ros87). We show that this protein, which bears important structural differences with respect to the eukaryotic domains, appears to structurally tolerate the zinc to cadmium substitution and the presence of cadmium does not affect the DNA binding activity of the protein. Moreover, we show for the first time how zinc to cadmium replacement can also take place in a cellular context. Our findings both complement and extend previous results obtained for different eukaryotic zinc fingers, suggesting that metal substitution in zinc fingers may be of relevance to the toxicity and/or carcinogenicity mechanisms of this metal. This journal is 2014 The Royal Society of Chemistry
Given the similar chemical properties of zinc and cadmium, zinc finger domains have been often proposed as mediators of the toxic and carcinogenic effects exerted by this xenobiotic metal. The effects of zinc replacement by cadmium in different eukaryotic zinc fingers have been reported. In the present work, to evaluate the effects of such substitution in the prokaryotic zinc finger, we report a detailed study of its functional and structural consequences on the Ros DNA binding domain (Ros87). We show that this protein, which bears important structural differences with respect to the eukaryotic domains, appears to structurally tolerate the zinc to cadmium substitution and the presence of cadmium does not affect the DNA binding activity of the protein. Moreover, we show for the first time how zinc to cadmium replacement can also take place in a cellular context. Our findings both complement and extend previous results obtained for different eukaryotic zinc fingers, suggesting that metal substitution in zinc fingers may be of relevance to the toxicity and/or carcinogenicity mechanisms of this metal. This journal is 2014 The Royal Society of Chemistry
Zinc To Cadmium Replacement In The Prokaryotic Zinc-Finger Domain
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Zinc To Cadmium Replacement In The Prokaryotic Zinc-Finger Domain
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Malgieri G, Zaccaro L, Leone M, Bucci E, Esposito S, Baglivo I, Del Gatto A, Russo L, Scandurra R, Pedone PV, Fattorusso R, Isernia C
* Zinc to Cadmium Replacement in the A. thaliana SUPERMAN Cys(2)His(2) Zinc Finger Induces Structural Rearrangements of Typical DNA Base Determinant Positions (504 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2011 Nov; 95(11): 801-810.
Impact Factor: 2.87
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Malgieri G, Russo L, Esposito S, Baglivo I, Zaccaro L, Pedone EM, Di Blasio B, Isernia C, Pedone PV, Fattorusso R
* The Prokaryotic Cys2his2 Zinc Finger Domain Adopts A Novel Fold As Revealed By The Solution Structure Of Agrobacterium Tumefaciens Ros Dna Binding Domain (571 views)
P Natl Acad Sci Usa (ISSN: 0027-8424, 1091-6490, 0027-8424print), 2007 Oct 30; 104(44): 17341-17346.
Impact Factor: 9.598
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Esposito S, Baglivo I, Malgieri G, Russo L, Zaccaro L, D'Andrea LD, Mammucari M, Di Blasio B, Isernia C, Fattorusso R, Pedone PV
* A novel type of zinc finger DNA binding domain in the Agrobacterium tumefaciens transcriptional regulator Ros (1073 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2006 Sep 29; 45(34): 10394-10405.
Impact Factor: 3.633
View Export to BibTeX Export to EndNote
* Zinc to Cadmium Replacement in the A. thaliana SUPERMAN Cys(2)His(2) Zinc Finger Induces Structural Rearrangements of Typical DNA Base Determinant Positions (504 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2011 Nov; 95(11): 801-810.
Impact Factor: 2.87
View Export to BibTeX Export to EndNote
Malgieri G, Russo L, Esposito S, Baglivo I, Zaccaro L, Pedone EM, Di Blasio B, Isernia C, Pedone PV, Fattorusso R
* The Prokaryotic Cys2his2 Zinc Finger Domain Adopts A Novel Fold As Revealed By The Solution Structure Of Agrobacterium Tumefaciens Ros Dna Binding Domain (571 views)
P Natl Acad Sci Usa (ISSN: 0027-8424, 1091-6490, 0027-8424print), 2007 Oct 30; 104(44): 17341-17346.
Impact Factor: 9.598
View Export to BibTeX Export to EndNote
Esposito S, Baglivo I, Malgieri G, Russo L, Zaccaro L, D'Andrea LD, Mammucari M, Di Blasio B, Isernia C, Fattorusso R, Pedone PV
* A novel type of zinc finger DNA binding domain in the Agrobacterium tumefaciens transcriptional regulator Ros (1073 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2006 Sep 29; 45(34): 10394-10405.
Impact Factor: 3.633
View Export to BibTeX Export to EndNote
3 Records (3 excluding Abstracts).
Total impact factor: 16.101 (16.101 excluding Abstracts).
Total 5 year impact factor: 16.172 (16.172 excluding Abstracts).
Total impact factor: 16.101 (16.101 excluding Abstracts).
Total 5 year impact factor: 16.172 (16.172 excluding Abstracts).
625 views. Last view on Friday 13 September 2024, 6:31:19
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