ArticlePloS one2012
Dimerization and heme binding are conserved in amphibian and starfish homologues of the microRNA processing protein DGCR8.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- The structural landscape of Microprocessor-mediated processing of pri-let-7 miRNAs.Molecular cell · 2024Article
- A transcription-independent role for HIF-1α in modulating microprocessor assembly.Nucleic acids research · 2024Article
- The structural landscape of Microprocessor mediated pri-bioRxiv : the preprint server for biology · 2024Article
- A Structural View of miRNA Biogenesis and Function.Non-coding RNA · 2022Review
- CO and NO bind to Fe(II) DiGeorge critical region 8 heme but do not restore primary microRNA processing activity.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Article
- Structural and functional insights into the fly microRNA biogenesis factor Loquacious.RNA (New York, N.Y.) · 2016Article
- A heterotrimer model of the complete Microprocessor complex revealed by single-molecule subunit counting.RNA (New York, N.Y.) · 2016Article
- The DGCR8 RNA-binding heme domain recognizes primary microRNAs by clamping the hairpin.Cell reports · 2014Article
- Processing of microRNA primary transcripts requires heme in mammalian cells.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Primary microRNA processing assay reconstituted using recombinant Drosha and DGCR8.Methods in molecular biology (Clifton, N.J.) · 2014Article
- MicroRNA Machinery Genes as Novel Biomarkers for Cancer.Frontiers in oncology · 2014Review
- Phosphorylation of DGCR8 increases its intracellular stability and induces a progrowth miRNA profile.Cell reports · 2013Article
- Pyridine Hemochromagen Assay for Determining the Concentration of Heme in Purified Protein Solutions.Bio-protocolArticle
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Authors and funding
5 authors.
Funding
Abstract
Human DiGeorge Critical Region 8 (DGCR8) is an essential microRNA (miRNA) processing factor that is activated via direct interaction with Fe(III) heme. In order for DGCR8 to bind heme, it must dimerize using a dimerization domain embedded within its heme-binding domain (HBD). We previously reported a crystal structure of the dimerization domain from human DGCR8, which demonstrated how dimerization results in the formation of a surface important for association with heme. Here, in an attempt to crystallize the HBD, we search for DGCR8 homologues and show that DGCR8 from Patiria miniata (bat star) also binds heme. The extinction coefficients (ε) of DGCR8-heme complexes are determined; these values are useful for biochemical analyses and allow us to estimate the heme occupancy of DGCR8 proteins. Additionally, we present the crystal structure of the Xenopus laevis dimerization domain. The structure is very similar to that of human DGCR8. Our results indicate that dimerization and heme binding are evolutionarily conserved properties of DGCR8 homologues not only in vertebrates, but also in at least some invertebrates.
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