Solution structure of the Drosha double-stranded RNA-binding domain

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Abstract

Background: Drosha is a nuclear RNase III enzyme that initiates processing of regulatory microRNA. Together with partner protein DiGeorge syndrome critical region 8 (DGCR8), it forms the Microprocessor complex, which cleaves precursor transcripts called primary microRNA to produce hairpin precursor microRNA. In addition to two RNase III catalytic domains, Drosha contains a C-terminal double-stranded RNA-binding domain (dsRBD). To gain insight into the function of this domain, we determined the nuclear magnetic resonance (NMR) solution structure.Results: We report here the solution structure of the dsRBD from Drosha (Drosha-dsRBD). The αβββα fold is similar to other dsRBD structures. A unique extended loop distinguishes this domain from other dsRBDs of known structure.Conclusions: Despite uncertainties about RNA-binding properties of the Drosha-dsRBD, its structure suggests it retains RNA-binding features. We propose that this domain may contribute to substrate recognition in the Drosha-DGCR8 Microprocessor complex. © 2010 Mueller et al; licensee BioMed Central Ltd.

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Mueller, G. A., Miller, M. T., DeRose, E. F., Ghosh, M., London, R. E., & Hall, T. M. T. (2010). Solution structure of the Drosha double-stranded RNA-binding domain. Silence, 1(1). https://doi.org/10.1186/1758-907X-1-2

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