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Bioinformatics Advance Access originally published online on September 5, 2006
Bioinformatics 2006 22(22):2711-2714; doi:10.1093/bioinformatics/btl468
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© 2006 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

DUF283 domain of Dicer proteins has a double-stranded RNA-binding fold

Mensur Dlakic

Department of Microbiology, Montana State University Bozeman, MT 59717, USA

Two RNases, Dicer and Argonaute, are at the heart of the RNA interference (RNAi) molecular machinery responsible for gene silencing. Both RNases contain multiple domains, most of which have been characterized or have functions that can be predicted based on sequence comparisons. However, Dicers of higher eukaryotes contain the domain known as DUF283 which at present has no assigned role. Using sensitive profile–profile comparisons, we detected a divergent double-stranded RNA-binding domain coinciding with the DUF283 of Dicer. This finding has potential implications regarding the mechanistic role of Dicer in RNAi.

Contact: mdlakic{at}montana.edu

Supplementary information: Supplementary images are available at Bioinformatics online.

Received on June 14, 2006; revised on August 7, 2006; accepted on August 29, 2006

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