Cited by 177DNA Repair MechanismsHeavy Metal Exposure and ToxicityArsenic contamination and mitigation

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Arsenite Interacts Selectively with Zinc Finger Proteins Containing C3H1 or C4 Motifs

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Zhou, Xixi, Sun, Xi, Cooper, Karen L., Wang, Feng, Liu, Ke Jian, Hudson, Laurie G.·2011·Journal of Biological Chemistry

DOI 10.1074/jbc.m111.232926PMC PMC3123053

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Abstract

Arsenic inhibits DNA repair and enhances the genotoxicity of DNA-damaging agents such as benzo[a]pyrene and ultraviolet radiation. Arsenic interaction with DNA repair proteins containing functional zinc finger motifs is one proposed mechanism to account for these observations. Here, we report that arsenite binds to both CCHC DNA-binding zinc fingers of the DNA repair protein PARP-1 (poly(ADP-ribose) polymerase-1). Furthermore, trivalent arsenite coordinated with all three cysteine residues as demonstrated by MS/MS. MALDI-TOF-MS analysis of peptides harboring site-directed substitutions of cysteine with histidine residues within the PARP-1 zinc finger revealed that arsenite bound to peptides containing three or four cysteine residues, but not to peptides with two cysteines, demonstrating arsenite binding selectivity. This finding was not unique to PARP-1; arsenite did not bind to a peptide representing the CCHH zinc finger of the DNA repair protein aprataxin, but did bind to an aprataxin peptide mutated to a CCHC zinc finger. To investigate the impact of arsenite on PARP-1 zinc finger function, we measured the zinc content and DNA-binding capacity of PARP-1 immunoprecipitated from arsenite-exposed cells. PARP-1 zinc content and DNA binding were decreased by 76 and 80%, respectively, compared with protein isolated from untreated cells. We observed comparable decreases in zinc content for XPA (xeroderma pigmentosum group A) protein (CCCC zinc finger), but not SP-1 (specificity protein-1) or aprataxin (CCHH zinc finger). These findings demonstrate that PARP-1 is a direct molecular target of arsenite and that arsenite interacts selectively with zinc finger motifs containing three or more cysteine residues.

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Self-citation

Authors: Zhou, X., Sun, X., Cooper, K. L., Wang, F., Liu, K. J., & Hudson, L. G.
Affiliations: University of New Mexico (US)
Corresponding author: Liu, Ke Jian
Hudson, Laurie G.
ORCID: Zhou, Xixi
Sun, Xi
Liu, Ke Jian
Hudson, Laurie G.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2011-07
Volume: 286
Issue: 26
Pages: 22855-22863
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m111.232926
PMC: PMC3123053
OpenAlex: W1986093310
Cited by: 177
References: 43
Citations by year: 2026: 6 · 2025: 5 · 2024: 4 · 2023: 12 · 2022: 12 · 2021: 7 · 2020: 17 · 2019: 8 · 2018: 12 · 2017: 16 · 2016: 14 · 2015: 22 · 2014: 14 · 2013: 13 · 2012: 12
FWCI: 5.46
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 3409 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (CA118100)
National Cancer Institute (P30CA118100)
National Institute of Environmental Health Sciences (R01ES15826-03S1, R01ES15826, R01ES015826)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Physical Sciences › Environmental Science › Health, Toxicology and Mutagenesis › Heavy Metal Exposure and Toxicity
Physical Sciences › Environmental Science › Environmental Chemistry › Arsenic contamination and mitigation
Keywords: arsenite, zinc finger proteins, PARP1, CCHC zinc finger, aprataxin, XPA, Sp1, cysteine residues, DNA repair proteins, genotoxicity
MeSH terms: Poly (ADP-Ribose) Polymerase-1, Cell Line, DNA-Binding Proteins, Humans, Mutation, Nuclear Proteins, Peptides, Poly(ADP-ribose) Polymerases, Protein Binding, Teratogens, Zinc Fingers, Arsenites

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Arsenite Interacts Selectively with Zinc Finger Proteins Containing C3H1 or C4 Motifs

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