University of Wroclaw, Faculty of Chemistry, 14F. Joliot-Curie St, Wroclaw, 50383, Poland.
University of Wroclaw, Faculty of Biological Sciences, Institute of Experimental Biology, 6 Kanonia St, Wroclaw, 50328, Poland.
Sci Rep. 2020 Mar 6;10(1):4196. doi: 10.1038/s41598-020-61145-5.
Tail Tubular Protein A (TTPA) was long thought to be strictly a structural protein of environmental bacteriophages. However, our recent work has suggested that some TTPAs have additional functional features and thus are dual-function proteins. This study introduces a new TTPA family member, TTPAgp11, which belongs to Yersinia phage phiYeO3-12. We cloned the gene, expressed it and then purified the phage protein. The protein, including its hydrolytic activity, was characterized. Our enzymatic activity tests showed that TTPAgp11 displayed hydrolytic activity towards Red-starch, suggesting that this enzyme could be classified as part as the α - 1, 4-glucosidase family. Protein folding and aggregation tests indicated that TTPAgp11 is a single-domain protein whose aggregation can be induced by maltose or N-acetylglucosamine. The spatial structure of TTPAgp11 seemed to resemble that of the first reported dual-function TTPA, TTPAgp31, which was isolated from Klebsiella pneumoniae phage 32.
尾管蛋白 A（TTPA）曾长期被认为是环境噬菌体的一种严格的结构蛋白。然而，我们最近的工作表明，一些 TTPA 具有额外的功能特征，因此是双功能蛋白。本研究介绍了一种新的 TTPA 家族成员，TTPAgp11，它属于耶尔森氏噬菌体 phiYeO3-12。我们克隆了该基因，表达并纯化了噬菌体蛋白。对该蛋白及其水解活性进行了表征。我们的酶活性测试表明，TTPAgp11 对红淀粉具有水解活性，表明该酶可归类为α-1,4-葡萄糖苷酶家族的一部分。蛋白折叠和聚集测试表明，TTPAgp11 是一种单结构域蛋白，其聚集可被麦芽糖或 N-乙酰葡萄糖胺诱导。TTPAgp11 的空间结构似乎类似于从肺炎克雷伯氏菌噬菌体 32 中分离到的第一个报道的双功能 TTPA，TTPAgp31。
