Transcriptomics

Dataset Information

179

An Extended dsRBD with a Novel Zinc-Binding Motif Mediates Nuclear Retention of Fission Yeast Dicer


ABSTRACT: Dicer proteins function in RNA interference (RNAi) pathways by generating small RNAs (sRNAs). Here we report the solution structure of the C-terminal domain of Schizosaccharomyces pombe Dicer (Dcr1). The structure reveals an unusual double-stranded RNA binding domain (dsRBD) fold embedding a novel zinc-binding motif that is conserved among dicers in yeast. Although the C-terminal domain of Dcr1 still binds nucleic acids, this property is dispensable for proper functioning of Dcr1. In contrast, disruption of zinc coordination renders Dcr1 mainly cytoplasmic and leads to remarkable changes in gene expression and loss of heterochromatin assembly. In summary, our results reveal novel insights into the mechanism of nuclear retention of Dcr1 and raise the possibility that this new class of dsRBDs might generally function in nucleo-cytoplasmic trafficking and not substrate binding. The C-terminal domain of Dcr1 constitutes a novel regulatory module that might represent a potential target for therapeutic intervention with fungal diseases. 12 chips representing 4 different strains. Every condition is represented by three biological replicates

ORGANISM(S): Schizosaccharomyces pombe  

SUBMITTER: Frédéric H Allain   Marc Bühler  Yukiko Shimada  Hans-Rudolf Hotz  Stephan Emmerth  Pierre Barraud 

PROVIDER: E-GEOD-30586 | ArrayExpress | 2011-09-22

SECONDARY ACCESSION(S): GSE30586PRJNA144571

REPOSITORIES: GEO, ArrayExpress

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Publications

An extended dsRBD with a novel zinc-binding motif mediates nuclear retention of fission yeast Dicer.

Barraud Pierre P   Emmerth Stephan S   Shimada Yukiko Y   Hotz Hans-Rudolf HR   Allain Frédéric H-T FH   Bühler Marc M  

The EMBO journal 20110816 20


Dicer proteins function in RNA interference (RNAi) pathways by generating small RNAs (sRNAs). Here, we report the solution structure of the C-terminal domain of Schizosaccharomyces pombe Dicer (Dcr1). The structure reveals an unusual double-stranded RNA binding domain (dsRBD) fold embedding a novel zinc-binding motif that is conserved among dicers in yeast. Although the C-terminal domain of Dcr1 still binds nucleic acids, this property is dispensable for proper functioning of Dcr1. In contrast,  ...[more]

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