A thermostable endonuclease III homolog from the archaeon Pyrobaculum aerophilum.
A thermostable endonuclease III homolog from the archaeon Pyrobaculum aerophilum.
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来自古细菌 Pyrobaculum aerophilum 的热稳定核酸内切酶 III 同源物。
DOI：
10.1093/nar/29.3.604
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发表时间：
2001
影响因子：
14.9
通讯作者：
Miller,JH
中科院分区：
文献类型：
--
作者：
Yang,H;Phan,IT;Fitz-Gibbon,S;Shivji,MK;Wood,RD;Clendenin,WM;Hyman,EC;Miller,JH
Pyrimidine adducts in cellular DNA arise from modification of the pyrimidine 5,6-double bond by oxidation, reduction or hydration. The biological outcome includes increased mutation rate and potential lethality. A major DNAN-glycosylase responsible for the excision of modified pyrimidine bases is the base excision repair (BER) glycosylase endonuclease III, for which functional homologs have been identified and characterized inEscherichia coli, yeast and humans. So far, little is known about how hyperthermophilic Archaea cope with such pyrimidine damage. Here we report characterization of an endonuclease III homolog, PaNth, from the hyperthermophilic archaeonPyrobaculum aerophilum, whose optimal growth temperature is 100°C. The predicted product of 223 amino acids shares significant sequence homology with several [4Fe-4S]-containing DNAN-glycosylases includingE.coliendonuclease III (EcNth). The histidine-tagged recombinant protein was expressed inE.coliand purified. Under optimal conditions of 80–160 mM NaCl and 70°C, PaNth displays DNA glycosylase/β-lyase activity with the modified pyrimidine base 5,6-dihydrothymine (DHT). This activity is enhanced when DHT is paired with G. Our data, showing the structural and functional similarity between PaNth and EcNth, suggests that BER of modified pyrimidines may be a conserved repair mechanism in Archaea. Conserved amino acid residues are identified for five subfamilies of endonuclease III/UV endonuclease homologs clustered by phylogenetic analysis.
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影响因子：
2.9
作者：
Asagoshi, K;Odawara, H;Ide, H
通讯作者：
Ide, H
DOI：
--
发表时间：
1982-03
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
B. Demple;S. Linn
通讯作者：
B. Demple;S. Linn
DOI：
10.1073/pnas.94.15.8010
发表时间：
1997-07-22
影响因子：
11.1
作者：
Radicella, JP;Dherin, C;Boiteux, S
通讯作者：
Boiteux, S
腺嘌呤-DNA 糖基化酶 MutY 的 C 端结构域赋予 8-氧代鸟嘌呤.腺嘌呤错配的特异性，并且可能是从 MutT（一种 8-氧代-dGTP 酶）进化而来。
影响因子：
2.9
作者：
D. M. Noll;A. Gogos;J. Granek;N. Clarke
通讯作者：
N. Clarke
DNA 中 5-甲酰尿嘧啶修复酶的鉴定
影响因子：
4.8
作者：
Qiu;I. Miyabe;Y. Matsumoto;K. Kino;H. Sugiyama;S. Yonei
通讯作者：
S. Yonei