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J. Cell Biol.,
Volume 142, Number 4, August 24, 1998 899-912
* Institute of Histology and Embryology, Faculty of Medicine, University of Lisbon, 1699 Lisboa Codex, Portugal;
and The coiled body is a distinct subnuclear domain enriched in small nuclear ribonucleoprotein particles (snRNPs) involved in processing of pre-mRNA.
Although the function of the coiled body is still unknown, current models propose that it may have a role in snRNP biogenesis, transport, or recycling. Here we
describe that anti-coilin antibodies promote a specific
disappearance of the coiled body in living human cells,
thus providing a novel tool for the functional analysis of
this structure. Monoclonal antibodies (mAbs) were
raised against recombinant human coilin, the major
structural protein of the coiled body. Four mAbs are shown to induce a progressive disappearance of coiled
bodies within ~6 h after microinjection into the nucleus
of HeLa cells. After their disappearance, coiled bodies
are not seen to re-form, although injected cells remain
viable for at least 3 d. Epitope mapping reveals that the
mAbs recognize distinct amino acid motifs scattered along the complete coilin sequence. By 24 and 48 h after injection of antibodies that promote coiled body disappearance, splicing snRNPs are normally distributed
in the nucleoplasm, the nucleolus remains unaffected,
and the cell cycle progresses normally. Furthermore, cells devoid of coiled bodies for ~24 h maintain the
ability to splice both adenoviral pre-mRNAs and transiently overexpressed human European Molecular Biology Laboratory, D-69117 Heidelberg, Germany
-globin transcripts. In
conclusion, within the time range of this study, no major nuclear abnormalities are detected after coiled body
disappearance.
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