A functional endonuclease Q exists in the bacterial domain

Identification and characterization of endonuclease Q from Bacillus pumilus

Miyako Shiraishi, Sonoko Ishino, Isaac Cann, Yoshizumi Ishino

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

DNA base deamination occurs spontaneously under physiological conditions and is promoted by high temperature. Therefore, hyperthermophiles are expected to have efficient repair systems of the deaminated bases in their genomes. Endonuclease Q (EndoQ) was originally identified from the hyperthermophlic archaeon, Pyrococcus furiosus, as a hypoxanthine-specific endonuclease recently. Further biochemical analyses revealed that EndoQ also recognizes uracil, xanthine, and the AP site in DNA, and is probably involved in a specific repair process for damaged bases. Initial phylogenetic analysis showed that an EndoQ homolog is found only in the Thermococcales and some of the methanogens in Archaea, and is not present in most members of the domains Bacteria and Eukarya. A better understanding of the distribution of the EndoQ-mediated repair system is, therefore, of evolutionary interest. We showed here that an EndoQ-like polypeptide from Bacillus pumilus, belonging to the bacterial domain, is functional and has similar properties with the archaeal EndoQs.

Original languageEnglish
Pages (from-to)931-937
Number of pages7
JournalBioscience, Biotechnology and Biochemistry
Volume81
Issue number5
DOIs
Publication statusPublished - Jan 1 2017

Fingerprint

Endonucleases
Bacilli
Repair
Archaea
Thermococcales
Pyrococcus furiosus
Methanogens
Deamination
Hypoxanthine
Xanthine
Uracil
DNA
Eukaryota
Bacillus pumilus
Bacteria
Genes
Genome
Peptides
Temperature

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

Cite this

@article{523cd331e532457bb7870d5a887d266f,
title = "A functional endonuclease Q exists in the bacterial domain: Identification and characterization of endonuclease Q from Bacillus pumilus",
abstract = "DNA base deamination occurs spontaneously under physiological conditions and is promoted by high temperature. Therefore, hyperthermophiles are expected to have efficient repair systems of the deaminated bases in their genomes. Endonuclease Q (EndoQ) was originally identified from the hyperthermophlic archaeon, Pyrococcus furiosus, as a hypoxanthine-specific endonuclease recently. Further biochemical analyses revealed that EndoQ also recognizes uracil, xanthine, and the AP site in DNA, and is probably involved in a specific repair process for damaged bases. Initial phylogenetic analysis showed that an EndoQ homolog is found only in the Thermococcales and some of the methanogens in Archaea, and is not present in most members of the domains Bacteria and Eukarya. A better understanding of the distribution of the EndoQ-mediated repair system is, therefore, of evolutionary interest. We showed here that an EndoQ-like polypeptide from Bacillus pumilus, belonging to the bacterial domain, is functional and has similar properties with the archaeal EndoQs.",
author = "Miyako Shiraishi and Sonoko Ishino and Isaac Cann and Yoshizumi Ishino",
year = "2017",
month = "1",
day = "1",
doi = "10.1080/09168451.2016.1277946",
language = "English",
volume = "81",
pages = "931--937",
journal = "Bioscience, Biotechnology and Biochemistry",
issn = "0916-8451",
publisher = "Japan Society for Bioscience Biotechnology and Agrochemistry",
number = "5",

}

TY - JOUR

T1 - A functional endonuclease Q exists in the bacterial domain

T2 - Identification and characterization of endonuclease Q from Bacillus pumilus

AU - Shiraishi, Miyako

AU - Ishino, Sonoko

AU - Cann, Isaac

AU - Ishino, Yoshizumi

PY - 2017/1/1

Y1 - 2017/1/1

N2 - DNA base deamination occurs spontaneously under physiological conditions and is promoted by high temperature. Therefore, hyperthermophiles are expected to have efficient repair systems of the deaminated bases in their genomes. Endonuclease Q (EndoQ) was originally identified from the hyperthermophlic archaeon, Pyrococcus furiosus, as a hypoxanthine-specific endonuclease recently. Further biochemical analyses revealed that EndoQ also recognizes uracil, xanthine, and the AP site in DNA, and is probably involved in a specific repair process for damaged bases. Initial phylogenetic analysis showed that an EndoQ homolog is found only in the Thermococcales and some of the methanogens in Archaea, and is not present in most members of the domains Bacteria and Eukarya. A better understanding of the distribution of the EndoQ-mediated repair system is, therefore, of evolutionary interest. We showed here that an EndoQ-like polypeptide from Bacillus pumilus, belonging to the bacterial domain, is functional and has similar properties with the archaeal EndoQs.

AB - DNA base deamination occurs spontaneously under physiological conditions and is promoted by high temperature. Therefore, hyperthermophiles are expected to have efficient repair systems of the deaminated bases in their genomes. Endonuclease Q (EndoQ) was originally identified from the hyperthermophlic archaeon, Pyrococcus furiosus, as a hypoxanthine-specific endonuclease recently. Further biochemical analyses revealed that EndoQ also recognizes uracil, xanthine, and the AP site in DNA, and is probably involved in a specific repair process for damaged bases. Initial phylogenetic analysis showed that an EndoQ homolog is found only in the Thermococcales and some of the methanogens in Archaea, and is not present in most members of the domains Bacteria and Eukarya. A better understanding of the distribution of the EndoQ-mediated repair system is, therefore, of evolutionary interest. We showed here that an EndoQ-like polypeptide from Bacillus pumilus, belonging to the bacterial domain, is functional and has similar properties with the archaeal EndoQs.

UR - http://www.scopus.com/inward/record.url?scp=85018591325&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85018591325&partnerID=8YFLogxK

U2 - 10.1080/09168451.2016.1277946

DO - 10.1080/09168451.2016.1277946

M3 - Article

VL - 81

SP - 931

EP - 937

JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

SN - 0916-8451

IS - 5

ER -