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Substrate specificity and action mechanism of the HerA-NurA nuclease from the hyperthermophilic archaeon Thermococcus kodakarensis
by
Ishino, Yoshizumi
, Uda, Keishiro
, Yamagami, Takeshi
, Ishino, Sonoko
, Gopalasingam, Chai C.
, Shigematsu, Hideki
, Gerle, Christoph
, Numata, Tomoyuki
in
archaea
/ Archaeal Proteins - chemistry
/ Archaeal Proteins - genetics
/ Archaeal Proteins - metabolism
/ Chromosomes
/ Deoxyribonucleases - chemistry
/ Deoxyribonucleases - genetics
/ Deoxyribonucleases - metabolism
/ Dna Recombination
/ DNA repair
/ Dna Repair Enzymes
/ Dna Repair in Extremophiles
/ DNA structure
/ DNA, Archaeal - metabolism
/ EM structure
/ end resection
/ Enzyme Function
/ Genetics and Molecular Biology
/ Homologous Recombination
/ Homologous Recombination Repair
/ Microbial Physiology and Genetics
/ Models, Molecular
/ Molecular modelling
/ Nuclease
/ Nucleases
/ Nucleotide sequence
/ Recombination Enzymes
/ Research Article
/ Single-stranded DNA
/ Substrate Specificity
/ Thermococcus - enzymology
/ Thermococcus - genetics
/ Thermococcus kodakarensis
/ translocase
/ Yeast
2026
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Substrate specificity and action mechanism of the HerA-NurA nuclease from the hyperthermophilic archaeon Thermococcus kodakarensis
by
Ishino, Yoshizumi
, Uda, Keishiro
, Yamagami, Takeshi
, Ishino, Sonoko
, Gopalasingam, Chai C.
, Shigematsu, Hideki
, Gerle, Christoph
, Numata, Tomoyuki
in
archaea
/ Archaeal Proteins - chemistry
/ Archaeal Proteins - genetics
/ Archaeal Proteins - metabolism
/ Chromosomes
/ Deoxyribonucleases - chemistry
/ Deoxyribonucleases - genetics
/ Deoxyribonucleases - metabolism
/ Dna Recombination
/ DNA repair
/ Dna Repair Enzymes
/ Dna Repair in Extremophiles
/ DNA structure
/ DNA, Archaeal - metabolism
/ EM structure
/ end resection
/ Enzyme Function
/ Genetics and Molecular Biology
/ Homologous Recombination
/ Homologous Recombination Repair
/ Microbial Physiology and Genetics
/ Models, Molecular
/ Molecular modelling
/ Nuclease
/ Nucleases
/ Nucleotide sequence
/ Recombination Enzymes
/ Research Article
/ Single-stranded DNA
/ Substrate Specificity
/ Thermococcus - enzymology
/ Thermococcus - genetics
/ Thermococcus kodakarensis
/ translocase
/ Yeast
2026
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Substrate specificity and action mechanism of the HerA-NurA nuclease from the hyperthermophilic archaeon Thermococcus kodakarensis
by
Ishino, Yoshizumi
, Uda, Keishiro
, Yamagami, Takeshi
, Ishino, Sonoko
, Gopalasingam, Chai C.
, Shigematsu, Hideki
, Gerle, Christoph
, Numata, Tomoyuki
in
archaea
/ Archaeal Proteins - chemistry
/ Archaeal Proteins - genetics
/ Archaeal Proteins - metabolism
/ Chromosomes
/ Deoxyribonucleases - chemistry
/ Deoxyribonucleases - genetics
/ Deoxyribonucleases - metabolism
/ Dna Recombination
/ DNA repair
/ Dna Repair Enzymes
/ Dna Repair in Extremophiles
/ DNA structure
/ DNA, Archaeal - metabolism
/ EM structure
/ end resection
/ Enzyme Function
/ Genetics and Molecular Biology
/ Homologous Recombination
/ Homologous Recombination Repair
/ Microbial Physiology and Genetics
/ Models, Molecular
/ Molecular modelling
/ Nuclease
/ Nucleases
/ Nucleotide sequence
/ Recombination Enzymes
/ Research Article
/ Single-stranded DNA
/ Substrate Specificity
/ Thermococcus - enzymology
/ Thermococcus - genetics
/ Thermococcus kodakarensis
/ translocase
/ Yeast
2026
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Substrate specificity and action mechanism of the HerA-NurA nuclease from the hyperthermophilic archaeon Thermococcus kodakarensis
Journal Article
Substrate specificity and action mechanism of the HerA-NurA nuclease from the hyperthermophilic archaeon Thermococcus kodakarensis
2026
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Overview
To understand the specific function of the HerA-NurA complex, which is believed to function in the end resection process to create a 3′-overhanging DNA for the following strand invasion in homologous recombination, we performed biochemical and structural analyses of this complex from a hyperthermophilic archaeon, Thermococcus kodakarensis , inhabiting a harsh environment where DNA is easily damaged. We found that the HerA-NurA complex cleaves both strands of double-stranded DNA in an exonucleolytic manner, regardless of the structure of the DNA end. Our structural analysis revealed the detailed characteristics of the nuclease activity exhibited by the HerA-NurA complex. Based on the presented information, it is unlikely that the HerA-NurA complex directly functions in end resection, but rather is involved in other functions, possibly in defense against viral infections.
Publisher
American Society for Microbiology,American Society for Microbiology (ASM)
Subject
/ Archaeal Proteins - chemistry
/ Archaeal Proteins - genetics
/ Archaeal Proteins - metabolism
/ Deoxyribonucleases - chemistry
/ Deoxyribonucleases - genetics
/ Deoxyribonucleases - metabolism
/ Genetics and Molecular Biology
/ Homologous Recombination Repair
/ Microbial Physiology and Genetics
/ Nuclease
/ Yeast
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