Preparation and Analysis of Drosha
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.
- Methods in High-Resolution, Array-Based Comparative Genomic Hybridization
- Application of the Invader RNA Assay to the Polarity of Vertebrate mRNA Decay
- Assaying Dicer-Mediated miRNA Maturation by Means of Fluorescent Substrates
- Delivery of DNA to Skin by Electroporation
- Exogenous Protein Expression in Xenopus Oocytes: Basic Procedures
- Orpheus Recombination: A Comprehensive Bacteriophage System for Murine Targeting Vector Construction by Transplacement
- Microbial Genome Analysis and Comparisons: Web-Based Protocols and Resources
- Restriction Landmark Genome Scanning for the Detection of Mutations
- Separation and Cryopreservation of Lymphocytes from Spleen and Lymph Node
- Production of Chimeras Derived from Murine Embryonic Stem Cells