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Vol. 12, Issue 10, 3046-3059, October 2001
Department of Oncology, University of Alberta, Cross Cancer
Institute, Edmonton, Alberta T6G 1Z2 Canada
DEAD box proteins are putative RNA helicases that function in all
aspects of RNA metabolism, including translation, ribosome biogenesis,
and pre-mRNA splicing. Because many processes involving RNA metabolism
are spatially organized within the cell, we examined the subcellular
distribution of a human DEAD box protein, DDX1, to identify possible
biological functions. Immunofluorescence labeling of DDX1 demonstrated
that in addition to widespread punctate nucleoplasmic labeling, DDX1 is
found in discrete nuclear foci ~0.5 µm in diameter. Costaining with
anti-Sm and anti-promyelocytic leukemia (PML) antibodies indicates that
DDX1 foci are frequently located next to Cajal (coiled) bodies and less
frequently, to PML bodies. Most importantly, costaining with
anti-CstF-64 antibody indicates that DDX1 foci colocalize with cleavage
bodies. By microscopic fluorescence resonance energy transfer,
we show that labeled DDX1 resides within a Förster distance of 10 nm of labeled CstF-64 protein in both the nucleoplasm and within
cleavage bodies. Coimmunoprecipitation analysis indicates that a
proportion of CstF-64 protein resides in the same complex as DDX1.
These studies are the first to identify a DEAD box protein associating
with factors involved in 3'-end cleavage and polyadenylation of
pre-mRNAs.
Online version of this article contains video
material for Figures 2 and 5. Online version is available at
www.molbiolcell.org.
*
Corresponding author. E-mail address:
rgodbout{at}ualberta.ca.
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