ArticleNucleic acids research1997
Mechanism of DNA transesterification by vaccinia topoisomerase: catalytic contributions of essential residues Arg-130, Gly-132, Tyr-136 and Lys-167.
Article in Nucleic acids research, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 65 citations in OpenAlex.
- Entirely enzymatic nanofabrication of DNA-protein conjugates.Nucleic acids research · 2017Article
- Characterization of DNA Binding by the Isolated N-Terminal Domain of Vaccinia Virus DNA Topoisomerase IB.Biochemistry · 2017Article
- Biochemical characterization of the topoisomerase domain of Methanopyrus kandleri topoisomerase V.The Journal of biological chemistry · 2014Article
- Chemical mutagenesis of vaccinia DNA topoisomerase lysine 167 provides insights to the catalysis of DNA transesterification.Biochemistry · 2013Article
- Mechanism and specificity of DNA strand exchange catalyzed by vaccinia DNA topoisomerase type I.Biochemistry · 2010Article
- A functional type I topoisomerase from Pseudomonas aeruginosa.BMC molecular biology · 2009Article
- Structural studies of type I topoisomerases.Nucleic acids research · 2009Review
- Chemical and traditional mutagenesis of vaccinia DNA topoisomerase provides insights to cleavage site recognition and transesterification chemistry.The Journal of biological chemistry · 2008Article
- New peptide inhibitors of type IB topoisomerases: similarities and differences vis-a-vis inhibitors of tyrosine recombinases.Journal of molecular biology · 2006Article
- Structure of the N-terminal fragment of topoisomerase V reveals a new family of topoisomerases.The EMBO journal · 2006Article
- Characterization of mimivirus DNA topoisomerase IB suggests horizontal gene transfer between eukaryal viruses and bacteria.Journal of virology · 2006Article
- A poxvirus-like type IB topoisomerase family in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Recombinogenic flap ligation pathway for intrinsic repair of topoisomerase IB-induced double-strand breaks.Molecular and cellular biology · 2000Article
- Vaccinia topoisomerase and Cre recombinase catalyze direct ligation of activated DNA substrates containing a 3'-para-nitrophenyl phosphate ester.Nucleic acids research · 2000Article
- Replacement of the active site tyrosine of vaccinia DNA topoisomerase by glutamate, cysteine or histidine converts the enzyme into a site-specific endonuclease.Nucleic acids research · 1998Article
- Intramolecular synapsis of duplex DNA by vaccinia topoisomerase.The EMBO journal · 1997Article
- Mutational analysis of vaccinia virus topoisomerase identifies residues involved in DNA binding.Nucleic acids research · 1997Article
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2 authors at 1 institution in 1 country.
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Abstract
Vaccinia topoisomerase, a eukaryotic type IB enzyme, catalyzes relaxation of supercoiled DNA by cleaving and rejoining DNA strands through a DNA- (3'-phosphotyrosyl)-enzyme intermediate. We have performed a kinetic analysis of mutational effects at four essential amino acids: Arg-130, Gly-132, Tyr-136 and Lys-167. Arg-130, Gly-132 and Lys-167 are conserved in all members of the type IB topoisomerase family. Tyr-136 is conserved in all poxvirus topoisomerases. We show that Arg-130 and Lys-167 are required for transesterification chemistry. Arg-130 enhances the rates of both cleavage and religation by 10(5). Lys-167 enhances the cleavage and religation reactions by 10(3) and 10(4), respectively. An instructive distinction between these two essential residues is that Arg-130 cannot be replaced by lysine, whereas substituting Lys-167 by arginine resulted in partial restoration of function relative to the alanine mutant. We propose that both basic residues interact directly with the scissile phosphate at the topoisomerase active site. Mutations at positions Gly-132 and Tyr-136 reduced the rate of strand cleavage by more than two orders of magnitude, but elicited only mild effects on religation rate. Gly-132 and Tyr-136 are suggested to facilitate a pre-cleavage activation step. The results of comprehensive mutagenesis of the vaccinia topoisomerase illuminate mechanistic and structural similarities to site-specific recombinases.
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