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MBC in Press, published online ahead of print September 7, 2005
Mol. Biol. Cell 10.1091/mbc.E05-06-0587

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Submitted on June 30, 2005
Revised on August 24, 2005
Accepted on August 25, 2005

P54nrb Forms a Heterodimer with PSP1 That Localizes to Paraspeckles in a RNA-dependent Manner

Archa H. Fox,* Charles S. Bond,{dagger} and Angus I. Lamond*

*Division of Gene Regulation and Expression and {dagger}Division of Biological Chemistry and Molecular Microbiology, Wellcome Trust Biocentre, University of Dundee, Dundee DD1 5EH, United Kingdom

Monitoring Editor: Joseph Gall

P54nrb is a protein implicated in multiple nuclear processes whose specific functions may correlate with its presence at different nuclear locations. Here we characterize paraspeckles, a subnuclear domain containing p54nrb and other RNA binding proteins including PSP1, a protein with sequence similarity to p54nrb that acts as a marker for paraspeckles. We show that PSP1 interacts in vivo with a subset of the total cellular pool of p54nrb. We map the domain within PSP1 that is mediating this interaction and show it is required for the correct localization of PSP1 to paraspeckles. This interaction is necessary but not sufficient for paraspeckle targeting by PSP1, which also requires an RRM capable of RNA binding. Blocking the reinitiation of RNA Pol II transcription at the end of mitosis with DRB prevents paraspeckle formation, which recommences after removal of DRB, indicating that paraspeckle formation is dependent upon RNA Polymerase II transcription. Thus paraspeckles are the sites where a subset of the total cellular pool of p54nrb is targeted in a RNA Polymerase II dependent manner.

Address correspondence to: Angus I. Lamond (a.i.lamond{at}dundee.ac.uk)




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