DOI Seite / Zitierlink:
https://doi.org/10.11588/diglit.48120#0021
Abstracts
3
Fibrillarin from Xenopus laevis'. cDNA Cloning and Expression Dur-
ing Development
M. Caizergues-Ferrer1, B. Lapeyre1, P. Mariotini2, C. Mathieu1, P. Ferrer1,
F. Amaldi2, F. Amalric1
'C.R.B.G. du C.N.R.S., 118 route de Narbonne, 31062 Toulouse, France
2Universita di Roma “Tor Vergata”, Rome, Italy
Fibrillarin is a glycine-dimethylarginine (DMA)-rich protein associated with
U3 RNA within a snRNP particle in the nucleolus of eukaryotic cells. We have
isolated a 1.6 kb long cDNA clone from a Xenopus laevis library by screening
with a DNA probe encoding a gly-DMA-rich domain in another nucleolar protein
(nucleolin). The protein sequence deduced from the sequence of the isolated clone
has been identified by comparison with that previously described for fibrillarin
from rat and Physarum polycephalum, and is shown to encode the whole protein.
As expected, the NH2-end of the protein exhibits a 79 long gly-DMA-rich do-
main. Moreover, this protein also exhibits a domain that could correspond to an
RNA binding domain, possessing an RNP consensus sequence. This result is in
agrement with the fact that the protein is known to be associated with U3 RNA.
The expression of fibrillarin has been followed throughout oogenesis and em-
bryogenesis. Fibrillarin is accumulated during oogenesis and its expression is not
under a translational control during early embryogenesis. Localization of
fibrillarin during development has been studied by indirect immunofluorescence.
Fibrillarin and nucleolin have been shown previously to be associated with the
nucleolus in interphase, and during at telophase both are present in the
prenucleolar bodies. We show here that, in addition to this localization, the two
proteins exhibit two common structural features: the presence of both gly-
DMA-rich and RNA binding domains.
Nuclear Receptors as Transcriptional Enhancers
P. Chambon
LGME/CNRS and U. 184/INSERM, Fac. Medecine, Strasbourg, France
Steroid/thyroid hormone and retinoic acid receptors are ligand-inducible
transcriptional enhancers which bind to specific cis-acting palindromic responsive
3
Fibrillarin from Xenopus laevis'. cDNA Cloning and Expression Dur-
ing Development
M. Caizergues-Ferrer1, B. Lapeyre1, P. Mariotini2, C. Mathieu1, P. Ferrer1,
F. Amaldi2, F. Amalric1
'C.R.B.G. du C.N.R.S., 118 route de Narbonne, 31062 Toulouse, France
2Universita di Roma “Tor Vergata”, Rome, Italy
Fibrillarin is a glycine-dimethylarginine (DMA)-rich protein associated with
U3 RNA within a snRNP particle in the nucleolus of eukaryotic cells. We have
isolated a 1.6 kb long cDNA clone from a Xenopus laevis library by screening
with a DNA probe encoding a gly-DMA-rich domain in another nucleolar protein
(nucleolin). The protein sequence deduced from the sequence of the isolated clone
has been identified by comparison with that previously described for fibrillarin
from rat and Physarum polycephalum, and is shown to encode the whole protein.
As expected, the NH2-end of the protein exhibits a 79 long gly-DMA-rich do-
main. Moreover, this protein also exhibits a domain that could correspond to an
RNA binding domain, possessing an RNP consensus sequence. This result is in
agrement with the fact that the protein is known to be associated with U3 RNA.
The expression of fibrillarin has been followed throughout oogenesis and em-
bryogenesis. Fibrillarin is accumulated during oogenesis and its expression is not
under a translational control during early embryogenesis. Localization of
fibrillarin during development has been studied by indirect immunofluorescence.
Fibrillarin and nucleolin have been shown previously to be associated with the
nucleolus in interphase, and during at telophase both are present in the
prenucleolar bodies. We show here that, in addition to this localization, the two
proteins exhibit two common structural features: the presence of both gly-
DMA-rich and RNA binding domains.
Nuclear Receptors as Transcriptional Enhancers
P. Chambon
LGME/CNRS and U. 184/INSERM, Fac. Medecine, Strasbourg, France
Steroid/thyroid hormone and retinoic acid receptors are ligand-inducible
transcriptional enhancers which bind to specific cis-acting palindromic responsive