Hansen Sarah R, Aderounmu Adedeji M, Donelick Helen M, Bass Brenda L
Department of Biochemistry, University of Utah, Salt Lake City, Utah 84112-5650, USA.
Cold Spring Harb Symp Quant Biol. 2019;84:185-193. doi: 10.1101/sqb.2019.84.039750. Epub 2020 Mar 16.
The function of Dicer's helicase domain has been enigmatic since its discovery. Why do only some Dicers require ATP, despite a high degree of sequence conservation in their helicase domains? We discuss evolutionary considerations based on differences between vertebrate and invertebrate antiviral defense, and how the helicase domain has been co-opted in extant organisms as the binding site for accessory proteins. Many accessory proteins are double-stranded RNA binding proteins, and we propose models for how they modulate Dicer function and catalysis.
自发现以来,Dicer解旋酶结构域的功能一直成谜。尽管其解旋酶结构域在序列上高度保守,但为何只有部分Dicer需要ATP呢?我们基于脊椎动物和无脊椎动物抗病毒防御的差异,探讨了进化方面的考量,以及解旋酶结构域在现存生物体中如何被用作辅助蛋白的结合位点。许多辅助蛋白都是双链RNA结合蛋白,我们提出了它们如何调节Dicer功能和催化作用的模型。