Abstract
Drosha is a member of the ribonuclease (RNase) III family. Like other RNase III proteins, Drosha is a double-stranded RNA (dsRNA)-specific endonuclease that introduces staggered cuts on each strand of the RNA helix (1,2). RNase III proteins are classified based on domain organization. Drosha and its homologs belong to class II, in which each member contains tandem RNase III catalytic motifs and one C-terminal dsRNA-binding domain (dsRBD) (3,4). Drosha also possesses an extended N-terminal domain whose function is currently unknown. Class I proteins are simpler and possess only one RNase III catalytic motif and a dsRNA-binding domain (dsRBD). The Dicer homologs of class III proteins contain a putative helicase domain, a PAZ domain, and a DUF283 domain apart from tandem nuclease domains and a dsRBD. The human genome encodes only two RNase III proteins: Drosha and Dicer. Whereas Dicer homologs are found in a broad range of eukaryotic organisms, Drosha homologs are present only in animals but not in yeast or plants.
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Acknowledgments
This work was supported by a grant (R02-2004-000-10173-0) from the Basic Research Program of the Korea Science & Engineering Foundation and by the BK21 Research Fellowship from the Ministry of Education and Human Resources Development.
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© 2005 Humana Press Inc.
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Lee, Y., Kim, V.N. (2005). Preparation and Analysis of Drosha. In: Carmichael, G.G. (eds) RNA Silencing. Methods in Molecular Biology™, vol 309. Humana Press. https://doi.org/10.1385/1-59259-935-4:017
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DOI: https://doi.org/10.1385/1-59259-935-4:017
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Print ISBN: 978-1-58829-436-4
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