Dicer’s Helicase Domain: A Meeting Place for Regulatory Proteins

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 def...

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Autores principales: HANSEN, SARAH R., ADEROUNMU, ADEDEJI M., DONELICK, HELEN M., BASS, BRENDA L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2020
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7384945/
https://www.ncbi.nlm.nih.gov/pubmed/32179591
http://dx.doi.org/10.1101/sqb.2019.84.039750
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author HANSEN, SARAH R.
ADEROUNMU, ADEDEJI M.
DONELICK, HELEN M.
BASS, BRENDA L.
author_facet HANSEN, SARAH R.
ADEROUNMU, ADEDEJI M.
DONELICK, HELEN M.
BASS, BRENDA L.
author_sort HANSEN, SARAH R.
collection PubMed
description 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.
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spelling pubmed-73849452021-03-16 Dicer’s Helicase Domain: A Meeting Place for Regulatory Proteins HANSEN, SARAH R. ADEROUNMU, ADEDEJI M. DONELICK, HELEN M. BASS, BRENDA L. Cold Spring Harb Symp Quant Biol Article 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. 2020-03-16 2019 /pmc/articles/PMC7384945/ /pubmed/32179591 http://dx.doi.org/10.1101/sqb.2019.84.039750 Text en http://creativecommons.org/licenses/by-nc/4.0/ This article is distributed under the terms of the Creative Commons Attribution-NonCommercial License, which permits reuse and redistribution, except for commercial purposes, provided that the original author and source are credited.
spellingShingle Article
HANSEN, SARAH R.
ADEROUNMU, ADEDEJI M.
DONELICK, HELEN M.
BASS, BRENDA L.
Dicer’s Helicase Domain: A Meeting Place for Regulatory Proteins
title Dicer’s Helicase Domain: A Meeting Place for Regulatory Proteins
title_full Dicer’s Helicase Domain: A Meeting Place for Regulatory Proteins
title_fullStr Dicer’s Helicase Domain: A Meeting Place for Regulatory Proteins
title_full_unstemmed Dicer’s Helicase Domain: A Meeting Place for Regulatory Proteins
title_short Dicer’s Helicase Domain: A Meeting Place for Regulatory Proteins
title_sort dicer’s helicase domain: a meeting place for regulatory proteins
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7384945/
https://www.ncbi.nlm.nih.gov/pubmed/32179591
http://dx.doi.org/10.1101/sqb.2019.84.039750
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