Journal article

Dimerization and Heme Binding Are Conserved in Amphibian and Starfish Homologues of the microRNA Processing Protein DGCR8

Rachel Senturia, Arthur Laganowsky, Ian Barr, Brooke D Scheidemantle, Feng Guo

PLOS ONE | PUBLIC LIBRARY SCIENCE | Published : 2012

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 va..

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University of Melbourne Researchers

Grants

Awarded by National Institutes of Health (NIH)


Awarded by NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES


Funding Acknowledgements

This work was supported by National Institutes of Health (NIH) grant GM080563 to F.G. and by UCLA Dissertation Year Fellowship to R.S. The funders had no role in the study design, data collection and analysis, decision to publish, or preparation of the manuscript.