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Dicer的解旋酶结构域：调控蛋白的汇聚场所。

Dicer's Helicase Domain: A Meeting Place for Regulatory Proteins.

作者信息

Hansen Sarah R, Aderounmu Adedeji M, Donelick Helen M, Bass Brenda L

机构信息

Department of Biochemistry, University of Utah, Salt Lake City, Utah 84112-5650, USA.

出版信息

Cold Spring Harb Symp Quant Biol. 2019;84:185-193. doi: 10.1101/sqb.2019.84.039750. Epub 2020 Mar 16.

DOI:10.1101/sqb.2019.84.039750
PMID:32179591
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7384945/
Abstract

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.

摘要

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。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/22ba/7384945/0c05c41599fd/nihms-1583811-f0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/22ba/7384945/adda64d74dc3/nihms-1583811-f0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/22ba/7384945/65fd4098945e/nihms-1583811-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/22ba/7384945/0c05c41599fd/nihms-1583811-f0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/22ba/7384945/adda64d74dc3/nihms-1583811-f0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/22ba/7384945/65fd4098945e/nihms-1583811-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/22ba/7384945/0c05c41599fd/nihms-1583811-f0003.jpg

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