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Title: Characterization of a Y-Family DNA Polymerase eta from the Eukaryotic Thermophile Alvinella pompejana

Abstract

Human DNA polymerase η (HsPol η ) plays an important role in translesion synthesis (TLS), which allows for replication past DNA damage such as UV-induced cis-syn cyclobutane pyrimidine dimers (CPDs). Here, we characterized ApPol η from the thermophilic worm Alvinella pompejana , which inhabits deep-sea hydrothermal vent chimneys. ApPol η shares sequence homology with HsPol η and contains domains for binding ubiquitin and proliferating cell nuclear antigen. Sun-induced UV does not penetrate Alvinella's environment; however, this novel DNA polymerase catalyzed efficient and accurate TLS past CPD, as well as 7,8-dihydro-8-oxoguanine and isomers of thymine glycol induced by reactive oxygen species. In addition, we found that ApPol η is more thermostable than HsPol η , as expected from its habitat temperature. Moreover, the activity of this enzyme was retained in the presence of a higher concentration of organic solvents. Therefore, ApPol η provides a robust, human-like Pol η that is more active after exposure to high temperatures and organic solvents.

Authors:
 [1];  [1];  [1];  [2];  [3];  [4];  [5];  [6];  [5];  [7];  [1]
  1. Graduate School of Engineering Science, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka 560-8531, Japan
  2. Graduate School of Engineering Science, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka 560-8531, Japan, Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA, Life Science Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA
  3. Life Science Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA, University of California San Diego, 9500 Gilman Drive no. 0613C, La Jolla, CA 92093, USA
  4. Life Science Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA
  5. Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA, Life Science Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA
  6. Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan
  7. Faculty of Science, Gakushuin University, 1-5-1 Mejiro, Toshima-ku, Tokyo 171-8588, Japan
Publication Date:
Sponsoring Org.:
USDOE
OSTI Identifier:
1198461
Grant/Contract Number:  
FG0207ER64326
Resource Type:
Published Article
Journal Name:
Journal of Nucleic Acids
Additional Journal Information:
Journal Name: Journal of Nucleic Acids Journal Volume: 2010; Journal ID: ISSN 2090-021X
Publisher:
Hindawi Publishing Corporation
Country of Publication:
Country unknown/Code not available
Language:
English

Citation Formats

Kashiwagi, Sayo, Kuraoka, Isao, Fujiwara, Yoshie, Hitomi, Kenichi, Cheng, Quen J., Fuss, Jill O., Shin, David S., Masutani, Chikahide, Tainer, John A., Hanaoka, Fumio, and Iwai, Shigenori. Characterization of a Y-Family DNA Polymerase eta from the Eukaryotic Thermophile Alvinella pompejana. Country unknown/Code not available: N. p., 2010. Web. doi:10.4061/2010/701472.
Kashiwagi, Sayo, Kuraoka, Isao, Fujiwara, Yoshie, Hitomi, Kenichi, Cheng, Quen J., Fuss, Jill O., Shin, David S., Masutani, Chikahide, Tainer, John A., Hanaoka, Fumio, & Iwai, Shigenori. Characterization of a Y-Family DNA Polymerase eta from the Eukaryotic Thermophile Alvinella pompejana. Country unknown/Code not available. doi:10.4061/2010/701472.
Kashiwagi, Sayo, Kuraoka, Isao, Fujiwara, Yoshie, Hitomi, Kenichi, Cheng, Quen J., Fuss, Jill O., Shin, David S., Masutani, Chikahide, Tainer, John A., Hanaoka, Fumio, and Iwai, Shigenori. Fri . "Characterization of a Y-Family DNA Polymerase eta from the Eukaryotic Thermophile Alvinella pompejana". Country unknown/Code not available. doi:10.4061/2010/701472.
@article{osti_1198461,
title = {Characterization of a Y-Family DNA Polymerase eta from the Eukaryotic Thermophile Alvinella pompejana},
author = {Kashiwagi, Sayo and Kuraoka, Isao and Fujiwara, Yoshie and Hitomi, Kenichi and Cheng, Quen J. and Fuss, Jill O. and Shin, David S. and Masutani, Chikahide and Tainer, John A. and Hanaoka, Fumio and Iwai, Shigenori},
abstractNote = {Human DNA polymerase η (HsPol η ) plays an important role in translesion synthesis (TLS), which allows for replication past DNA damage such as UV-induced cis-syn cyclobutane pyrimidine dimers (CPDs). Here, we characterized ApPol η from the thermophilic worm Alvinella pompejana , which inhabits deep-sea hydrothermal vent chimneys. ApPol η shares sequence homology with HsPol η and contains domains for binding ubiquitin and proliferating cell nuclear antigen. Sun-induced UV does not penetrate Alvinella's environment; however, this novel DNA polymerase catalyzed efficient and accurate TLS past CPD, as well as 7,8-dihydro-8-oxoguanine and isomers of thymine glycol induced by reactive oxygen species. In addition, we found that ApPol η is more thermostable than HsPol η , as expected from its habitat temperature. Moreover, the activity of this enzyme was retained in the presence of a higher concentration of organic solvents. Therefore, ApPol η provides a robust, human-like Pol η that is more active after exposure to high temperatures and organic solvents.},
doi = {10.4061/2010/701472},
journal = {Journal of Nucleic Acids},
number = ,
volume = 2010,
place = {Country unknown/Code not available},
year = {2010},
month = {1}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record
DOI: 10.4061/2010/701472

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