Department of Biochemistry, The University of Western Ontario, 1151 Richmond Street, London, ON N6A 5C1, Canada.
Department of Chemistry and Biochemistry, Center for RNA Biology, Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA.
Genes (Basel). 2019 Mar 26;10(3):250. doi: 10.3390/genes10030250.
The tRNA guanylyltransferase (Thg1) superfamily includes enzymes that are found in all three domains of life that all share the common ability to catalyze the 3' to 5' synthesis of nucleic acids. This catalytic activity, which is the reverse of all other known DNA and RNA polymerases, makes this enzyme family a subject of biological and mechanistic interest. Previous biochemical, structural, and genetic investigations of multiple members of this family have revealed that Thg1 enzymes use the 3' to 5' chemistry for multiple reactions in biology. Here, we describe the current state of knowledge regarding the catalytic features and biological functions that have been so far associated with Thg1 and its homologs. Progress toward the exciting possibility of utilizing this unusual protein activity for applications in biotechnology is also discussed.
tRNA 鸟苷酰转移酶(Thg1)超家族包括存在于所有三个生命领域的酶,它们都具有催化核酸 3' 到 5' 合成的共同能力。这种催化活性与所有其他已知的 DNA 和 RNA 聚合酶相反,使这个酶家族成为生物学和机制学研究的对象。对这个家族的多个成员进行的以前的生化、结构和遗传研究表明,Thg1 酶在生物学中使用 3' 到 5' 化学进行多种反应。在这里,我们描述了迄今为止与 Thg1 及其同源物相关的催化特征和生物学功能的现有知识状态。还讨论了利用这种不寻常的蛋白质活性在生物技术中的应用的令人兴奋的可能性的进展。