Characterization of a Y-Family DNA Polymerase eta from the Eukaryotic Thermophile Alvinella pompejana
Human DNA polymerase η (HsPolη) 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 ApPolη from the thermophilic worm Alvinella pompejana, which inhabits deep-sea...
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| Format: | Article |
| Language: | English |
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Wiley
2010-01-01
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| Series: | Journal of Nucleic Acids |
| Online Access: | http://dx.doi.org/10.4061/2010/701472 |
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| author | Sayo Kashiwagi Isao Kuraoka Yoshie Fujiwara Kenichi Hitomi Quen J. Cheng Jill O. Fuss David S. Shin Chikahide Masutani John A. Tainer Fumio Hanaoka Shigenori Iwai |
| author_facet | Sayo Kashiwagi Isao Kuraoka Yoshie Fujiwara Kenichi Hitomi Quen J. Cheng Jill O. Fuss David S. Shin Chikahide Masutani John A. Tainer Fumio Hanaoka Shigenori Iwai |
| author_sort | Sayo Kashiwagi |
| collection | DOAJ |
| description | Human DNA polymerase η (HsPolη) 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 ApPolη from the thermophilic worm Alvinella pompejana, which inhabits deep-sea hydrothermal vent chimneys. ApPolη shares sequence homology with HsPolη 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 ApPolη is more thermostable than HsPolη, 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, ApPolη provides a robust, human-like Polη that is more active after exposure to high temperatures and organic solvents. |
| format | Article |
| id | doaj-art-b1aa0d079d1b4a6eb756cdd3ce8515eb |
| institution | Kabale University |
| issn | 2090-021X |
| language | English |
| publishDate | 2010-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Journal of Nucleic Acids |
| spelling | doaj-art-b1aa0d079d1b4a6eb756cdd3ce8515eb2025-02-03T05:59:23ZengWileyJournal of Nucleic Acids2090-021X2010-01-01201010.4061/2010/701472701472Characterization of a Y-Family DNA Polymerase eta from the Eukaryotic Thermophile Alvinella pompejanaSayo Kashiwagi0Isao Kuraoka1Yoshie Fujiwara2Kenichi Hitomi3Quen J. Cheng4Jill O. Fuss5David S. Shin6Chikahide Masutani7John A. Tainer8Fumio Hanaoka9Shigenori Iwai10Graduate School of Engineering Science, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka 560-8531, JapanGraduate School of Engineering Science, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka 560-8531, JapanGraduate School of Engineering Science, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka 560-8531, JapanGraduate School of Engineering Science, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka 560-8531, JapanLife Science Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USALife Science Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USADepartment of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USAGraduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871, JapanDepartment of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USAFaculty of Science, Gakushuin University, 1-5-1 Mejiro, Toshima-ku, Tokyo 171-8588, JapanGraduate School of Engineering Science, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka 560-8531, JapanHuman DNA polymerase η (HsPolη) 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 ApPolη from the thermophilic worm Alvinella pompejana, which inhabits deep-sea hydrothermal vent chimneys. ApPolη shares sequence homology with HsPolη 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 ApPolη is more thermostable than HsPolη, 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, ApPolη provides a robust, human-like Polη that is more active after exposure to high temperatures and organic solvents.http://dx.doi.org/10.4061/2010/701472 |
| spellingShingle | Sayo Kashiwagi Isao Kuraoka Yoshie Fujiwara Kenichi Hitomi Quen J. Cheng Jill O. Fuss David S. Shin Chikahide Masutani John A. Tainer Fumio Hanaoka Shigenori Iwai Characterization of a Y-Family DNA Polymerase eta from the Eukaryotic Thermophile Alvinella pompejana Journal of Nucleic Acids |
| title | Characterization of a Y-Family DNA Polymerase eta from the Eukaryotic Thermophile Alvinella pompejana |
| title_full | Characterization of a Y-Family DNA Polymerase eta from the Eukaryotic Thermophile Alvinella pompejana |
| title_fullStr | Characterization of a Y-Family DNA Polymerase eta from the Eukaryotic Thermophile Alvinella pompejana |
| title_full_unstemmed | Characterization of a Y-Family DNA Polymerase eta from the Eukaryotic Thermophile Alvinella pompejana |
| title_short | Characterization of a Y-Family DNA Polymerase eta from the Eukaryotic Thermophile Alvinella pompejana |
| title_sort | characterization of a y family dna polymerase eta from the eukaryotic thermophile alvinella pompejana |
| url | http://dx.doi.org/10.4061/2010/701472 |
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