Characterization of a Y-Family DNA Polymerase eta from the Eukaryotic Thermophile Alvinella pompejana
| Autor: | John A. Tainer, Fumio Hanaoka, Quen J. Cheng, Kenichi Hitomi, Chikahide Masutani, David S. Shin, Jill O. Fuss, Isao Kuraoka, Yoshie Fujiwara, Shigenori Iwai, Sayo Kashiwagi |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2010 |
| Předmět: |
lcsh:QH426-470
Article Subject DNA damage DNA polymerase Pyrimidine dimer Biochemistry lcsh:Biochemistry 03 medical and health sciences 0302 clinical medicine lcsh:QD415-436 Molecular Biology Gene Polymerase 030304 developmental biology Genetics 0303 health sciences biology Thermophile biology.organism_classification Proliferating cell nuclear antigen lcsh:Genetics biology.protein Alvinella pompejana 030217 neurology & neurosurgery Research Article |
| Zdroj: | Journal of Nucleic Acids, Vol 2010 (2010) Journal of Nucleic Acids |
| DOI: | 10.4061/2010/701472 |
| Popis: | Human DNA polymeraseη(HsPolη) plays an important role in translesion synthesis (TLS), which allows for replication past DNA damage such as UV-inducedcis-syncyclobutane pyrimidine dimers (CPDs). Here, we characterized ApPolηfrom the thermophilic wormAlvinella pompejana, which inhabits deep-sea hydrothermal vent chimneys. ApPolηshares sequence homology with HsPolηand contains domains for binding ubiquitin and proliferating cell nuclear antigen. Sun-induced UV does not penetrateAlvinella'senvironment; 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 ApPolηis 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, ApPolηprovides a robust, human-like Polηthat is more active after exposure to high temperatures and organic solvents. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|