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Department of Embryology, Carnegie Institution, Baltimore, Maryland
21210
Coiled bodies (CBs) in the amphibian oocyte nucleus are spherical
structures up to 10 µm or more in diameter, much larger than their
somatic counterparts, which rarely exceed 1 µm. Oocyte CBs may have
smaller granules attached to their surface or embedded within them,
which are identical in structure and composition to the many hundreds
of B-snurposomes found free in the nucleoplasm. The matrix of the
CBs contains the diagnostic protein p80-coilin, which is colocalized
with the U7 small nuclear ribonucleoprotein (snRNP), whereas the
attached and embedded B-snurposomes contain splicing snRNPs. A few of
the 50-100 CBs in the oocyte nucleus are attached to lampbrush
chromosomes at the histone gene loci. By coimmunoprecipitation we show
that coilin and the U7 snRNP can form a weak but specific complex in
the nucleoplasm, which is dependent on the special U7 Sm-binding
site. Under the same conditions coilin does not associate with the U1
and U2 snRNPs. Coilin is a nucleic acid-binding protein, as shown by
its interaction with single-stranded DNA and with poly r(U) and poly
r(G). We suggest that an important function of coilin is to form a
transient complex with the U7 snRNP and accompany it to the CBs. In the case of CBs attached to chromosomes at the histone gene loci, the U7
snRNP is thus brought close to the actual site of histone pre-mRNA
transcription.
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