Maeda Y, Ueda H, Kazami J, Kawano G, Suzuki E, Nagamune T
Department of Chemistry and Biotechnology, Graduate School of Engineering, University of Tokyo.
J Biochem. 1996 Apr;119(4):601-3. doi: 10.1093/oxfordjournals.jbchem.a021284.
Significant amino acid sequence homology in two regions of Vargula hilgendorfii to one in apoaequorin was reported. The intra-amino acid homology in Vargula luciferase between residues 81-312 and 321-540 was 19.3%, and each of this intra-homologous region contained the region homologous to apoaequorin. In order to prove the possibility that only one of the homologous regions is sufficient for luminescence, we have produced a chimeric protein comprising of only the N-terminal homologous region of Vargula luciferase fused to protein A. Comparison of the luminescence of this truncate luciferase indicated that there was 38.5% retention in the bioluminescence of luciferase when compared to that of the mature form of luciferase. This fact may have interesting implications for further study of engineering luciferase.
据报道，希氏螣两个区域的氨基酸序列与脱辅基水母发光蛋白的一个区域具有显著的同源性。希氏螣荧光素酶81-312位残基与321-540位残基之间的氨基酸同源性为19.3%，每个同源区域都包含与脱辅基水母发光蛋白同源的区域。为了证明只有一个同源区域足以产生发光的可能性，我们制备了一种嵌合蛋白，该蛋白仅由希氏螣荧光素酶的N端同源区域与蛋白A融合而成。对这种截短型荧光素酶发光的比较表明，与成熟形式的荧光素酶相比，其生物发光保留了38.5%。这一事实可能对荧光素酶工程的进一步研究具有有趣的启示。
