嗜热栖热菌HB27中一种热稳定DNA光解酶的特性分析
Characterization of a thermostable DNA photolyase from an extremely thermophilic bacterium, Thermus thermophilus HB27.
作者信息
Kato R, Hasegawa K, Hidaka Y, Kuramitsu S, Hoshino T
机构信息
Department of Biology, Graduate School of Science, Osaka University, Toyonaka, Japan.
出版信息
J Bacteriol. 1997 Oct;179(20):6499-503. doi: 10.1128/jb.179.20.6499-6503.1997.
Abstract
The photolyase gene from Thermus thermophilus was cloned and sequenced. The characteristic absorption and fluorescence spectra of the purified T. thermophilus photolyase suggested that the protein has flavin adenine dinucleotide as a chromophore. The second chromophore binding site was not conserved in T. thermophilus photolyase. The purified enzyme showed light-dependent photoreactivation activity in vitro at 35 and 65 degrees C and was stable when subjected to heat and acidic pH.
摘要
克隆并测序了嗜热栖热菌的光解酶基因。纯化后的嗜热栖热菌光解酶的特征吸收光谱和荧光光谱表明，该蛋白质以黄素腺嘌呤二核苷酸作为发色团。嗜热栖热菌光解酶中第二个发色团结合位点并不保守。纯化后的酶在35摄氏度和65摄氏度下体外表现出光依赖的光复活活性，并且在受热和酸性pH条件下仍保持稳定。
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