ArticleNucleic acids research2002
The zinc ion in the HNH motif of the endonuclease domain of colicin E7 is not required for DNA binding but is essential for DNA hydrolysis.
Article in Nucleic acids research, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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25 citing papers in PubMed, 59 citations in OpenAlex.
- Versatile NTP recognition and domain fusions expand the functional repertoire of the ParB-CTPase fold beyond chromosome segregation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Hydrolytic Mechanism of a Metalloenzyme Is Modified by the Nature of the Coordinated Metal Ion.Molecules (Basel, Switzerland) · 2023Article
- Colicins and Microcins Produced byInternational journal of environmental research and public health · 2022Review
- Molecular Structure and Functional Analysis of Pyocin S8 from Pseudomonas aeruginosa Reveals the Essential Requirement of a Glutamate Residue in the H-N-H Motif for DNase Activity.Journal of bacteriology · 2020Article
- WSL9 Encodes an HNH Endonuclease Domain-Containing Protein that Is Essential for Early Chloroplast Development in Rice.Rice (New York, N.Y.) · 2020Article
- A structural study of TatD fromIUCrJ · 2020Article
- HK97 gp74 Possesses an α-Helical Insertion in the ββα Fold That Affects Its Metal Binding,Journal of bacteriology · 2020Article
- The effects of electroporation buffer composition on cell viability and electro-transfection efficiency.Scientific reports · 2020Article
- Functional and comparative genome analysis of novel virulent actinophages belonging to Streptomyces flavovirens.BMC microbiology · 2017Article
- Structural and functional characterization of deep-sea thermophilic bacteriophage GVE2 HNH endonuclease.Scientific reports · 2017Article
- Intrinsic protein disorder could be overlooked in cocrystallization conditions: An SRCD case study.Protein science : a publication of the Protein Society · 2016Article
- Substrate binding activates the designed triple mutant of the colicin E7 metallonuclease.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- Fine tuning of the catalytic activity of colicin E7 nuclease domain by systematic N-terminal mutations.Protein science : a publication of the Protein Society · 2014Article
- Increasing cleavage specificity and activity of restriction endonuclease KpnI.Nucleic acids research · 2013Article
- The role of the N-terminal loop in the function of the colicin E7 nuclease domain.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013Article
- Bacillus subtilis hlpB encodes a conserved stand-alone HNH nuclease-like protein that is essential for viability unless the hlpB deletion is accompanied by the deletion of genes encoding the AddAB DNA repair complex.Journal of bacteriology · 2012Article
- The protein gp74 from the bacteriophage HK97 functions as a HNH endonuclease.Protein science : a publication of the Protein Society · 2012Article
- Annealing helicase 2 (AH2), a DNA-rewinding motor with an HNH motif.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Cofactor requirement of HpyAV restriction endonuclease.PloS one · 2010Article
- Colicin biology.Microbiology and molecular biology reviews : MMBR · 2007Review
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7 authors at 1 institution in 1 country.
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Abstract
The HNH motif was originally identified in the subfamily of HNH homing endonucleases, which initiate the process of the insertion of mobile genetic elements into specific sites. Several bacteria toxins, including colicin E7 (ColE7), also contain the 30 amino acid HNH motif in their nuclease domains. In this work, we found that the nuclease domain of ColE7 (nuclease-ColE7) purified from Escherichia coli contains a one-to-one stoichiometry of zinc ion and that this zinc-containing enzyme hydrolyzes DNA without externally added divalent metal ions. The apo-enzyme, in which the indigenous zinc ion was removed from nuclease-ColE7, had no DNase activity. Several divalent metal ions, including Ni2+, Mg2+, Co2+, Mn2+, Ca2+, Sr2+, Cu2+ and Zn2+, re-activated the DNase activity of the apo-enzyme to various degrees, however higher concentrations of zinc ion inhibited this DNase activity. Two charged residues located at positions close to the zinc-binding site were mutated to alanine. The single-site mutants, R538A and E542A, showed reduced DNase activity, whereas the double-point mutant, R538A + E542A, had no observable DNase activity. A gel retardation assay further demonstrated that the nuclease-ColE7 hydrolyzed DNA in the presence of zinc ions, but only bound to DNA in the absence of zinc ions. These results demonstrate that the zinc ion in the HNH motif of nuclease-ColE7 is not required for DNA binding, but is essential for DNA hydrolysis, suggesting that the zinc ion not only stabilizes the folding of the enzyme, but is also likely to be involved in DNA hydrolysis.
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