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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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7384945 | PMC |
http://dx.doi.org/10.1101/sqb.2019.84.039750 | DOI Listing |
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