scholarly journals Actions of Agonists, Fipronil and Ivermectin on the Predominant In Vivo Splice and Edit Variant (RDLbd, I/V) of the Drosophila GABA Receptor Expressed in Xenopus laevis Oocytes

PLoS ONE ◽  
2014 ◽  
Vol 9 (5) ◽  
pp. e97468 ◽  
Author(s):  
Kristin Lees ◽  
Maria Musgaard ◽  
Siros Suwanmanee ◽  
Steven David Buckingham ◽  
Philip Biggin ◽  
...  
Keyword(s):  
Xenopus Laevis ◽  
Gaba Receptor ◽  
Xenopus Laevis Oocytes

Purification of a p47 phosphoprotein from Xenopus laevis oocytes and identification as an in vivo and in vitro p34cdc2 substrate

FEBS Letters ◽  
1989 ◽  
Vol 251 (1-2) ◽  
pp. 219-224 ◽  
Author(s):  
Odile Mulner-Lorillon ◽  
Robert Poulhe ◽  
Patrick Cormier ◽  
Jean-Claude Labbe ◽  
Marcel Doree ◽  
...  
Keyword(s):  
Xenopus Laevis ◽  
Xenopus Laevis Oocytes

scholarly journals Using in vivo imaging to measure RNA mobility in Xenopus laevis oocytes

Methods ◽  
2016 ◽  
Vol 98 ◽  
pp. 60-65 ◽  
Author(s):  
Erin A. Powrie ◽  
Veronica Ciocanel ◽  
Jill A. Kreiling ◽  
James A. Gagnon ◽  
Bjӧrn Sandstede ◽  
...  
Keyword(s):  
Xenopus Laevis ◽  
In Vivo Imaging ◽  
Xenopus Laevis Oocytes

Post-transcriptional regulation of ornithine decarboxylase in Xenopus laevis oocytes

Development ◽  
1990 ◽  
Vol 110 (3) ◽  
pp. 955-962 ◽  
Author(s):  
T. Bassez ◽  
J. Paris ◽  
F. Omilli ◽  
C. Dorel ◽  
H.B. Osborne
Keyword(s):  
Xenopus Laevis ◽  
Ornithine Decarboxylase ◽  
Stage Iv ◽  
Stage I ◽  
Northern Analysis ◽  
Xenopus Laevis Oocytes ◽  
Temporal Expression ◽  
Post Transcriptional Regulation ◽  
Translational Level

The level at which ornithine decarboxylase expression is regulated in growing oocytes has been investigated. Immunoprecipitation of the in vivo labelled proteins showed that ornithine decarboxylase accumulated less rapidly in stage IV oocytes than in previtellogenic stage I + II oocytes. Quantitative Northern analysis showed that ornithine decarboxylase mRNA is abundant in oocytes (about 8 × 10(8) transcripts/cell) and this number does not significantly change during oogenesis. Polysome analysis showed that this mRNA is present in polysomes in stage I + II oocytes but has passed into puromycin-insensitive mRNP particles by stage IV of oogenesis. Therefore, during the growth phase of oogenesis, ornithine decarboxylase expression is regulated at a translational level. These results are discussed relative to the temporal expression of ornithine decarboxylase and of other proteins whose expression also decreases during oogenesis. In order to perform these experiments, the cDNA (XLODC1) corresponding to Xenopus laevis ornithine decarboxylase mRNA was cloned and sequenced.

Xenopus laevis oocytes, eggs and tadpoles contain immunoactive insulin

1994 ◽  
Vol 141 (1) ◽  
pp. 123-129 ◽  
Author(s):  
F de Pablo ◽  
R Dashner ◽  
A R Shuldiner ◽  
J Roth
Keyword(s):  
Xenopus Laevis ◽  
High Performance ◽  
Immunoblot Analysis ◽  
Reversed Phase ◽  
Xenopus Laevis Oocytes ◽  
Maternal Origin ◽  
Insulin Mrna ◽  
Low Levels

Abstract Insulin is a multifunctional polypeptide hormone that regulates metabolic processes and promotes mitogenesis and differentiation in vitro in the cells and tissues of several species. Its role in vivo during embryogenesis is still poorly understood. We have previously found insulin mRNA in mature Xenopus laevis oocytes and in embryos during neurulation (before organogenesis of the pancreas takes place). We have now measured insulin immunoactivity in mature oocytes, unfertilized eggs and day-2 tadpoles. Using reversed phase high performance liquid chromatography, we found low levels of insulin in extracts of oocytes (stage VI). Both Xenopus insulin I and II were detected in unfertilized eggs. The day-2 tadpoles (stages 31–33) also contained immunoactive insulin, and in swimming tadpoles (stage 46) a few clusters of cells containing insulin immunoactivity could be identified by indirect immunofluorescence. Immunoblot analysis was relatively insensitive, detecting insulin only in the adult Xenopus pancreas. In summary, insulin (from maternal origin and embryonic expression) appears to be present early enough in Xenopus laevis to influence developmental processes such as neurulation. Journal of Endocrinology (1994) 141, 123–129

Accurate in vitro transcription of Xenopus laevis mitochondrial DNA from two bidirectional promoters

1986 ◽  
Vol 6 (7) ◽  
pp. 2543-2550
Author(s):  
D F Bogenhagen ◽  
B K Yoza
Keyword(s):  
Mitochondrial Dna ◽  
Xenopus Laevis ◽  
Rna Polymerase ◽  
Consensus Sequence ◽  
In Vitro Transcription ◽  
Xenopus Laevis Oocytes ◽  
Mitochondrial Rna ◽  
Bidirectional Promoters

The mitochondrial RNA polymerase from Xenopus laevis oocytes was partially purified by heparin-Sepharose chromatography and phosphocellulose chromatography. This RNA polymerase preparation specifically initiated the transcription of X. laevis mitochondrial DNA (mtDNA) from two bidirectional promoters contained within a 123-base-pair segment of the mtDNA between the heavy-strand replication origin and the rRNA cistrons. Transcription in vitro initiated from precisely the same start sites previously mapped as initiation sites for transcription in vivo. At each of the four sites, initiation occurred within a conserved nucleotide sequence, ACPuTTATA. This consensus sequence is not related to promoters for transcription of human mtDNA.

High tyrosinase activity in albino Xenopus laevis oocytes

Development ◽  
1976 ◽  
Vol 36 (3) ◽  
pp. 555-559
Author(s):  
A. H. Wyllie ◽  
E. M. De Robertis
Keyword(s):  
Molecular Weight ◽  
Xenopus Laevis ◽  
Specific Activity ◽  
High Specific Activity ◽  
Low Molecular Weight ◽  
Xenopus Laevis Oocytes ◽  
Melanin Synthesis ◽  
Wild Type ◽  
Albino Mutant

Tyrosinase was measured in oocytes of the recently described albino mutant (avav) of Xenopus laevis. Although these oocytes show no pigmentation and the eggs are known to contain no melanosomes, tyrosinase — which is probably the only enzyme necessary for melanin synthesis from tyrosine — was increased more than twofold relative to the wild type. Tyrosinase recovered from albino and wild type oocytes showed the same KM with respect to tyrosine, and this was not altered by previous gonadotrophin stimulation in vivo. The tyrosi-nase assay, based on [14]tyrosine incorporation into acid-insoluble products, was of greater sensitivity than previously described methods of the same type, through removal of low molecular weight material from the oocyte homogenate prior to incubation, and the use of tyrosine of high specific activity.

scholarly journals 3'-end-dependent formation of U6 small nuclear ribonucleoprotein particles in Xenopus laevis oocyte nuclei.

1992 ◽  
Vol 12 (7) ◽  
pp. 3032-3040 ◽  
Author(s):  
M P Terns ◽  
E Lund ◽  
J E Dahlberg
Keyword(s):  
Xenopus Laevis ◽  
Nuclear Antigen ◽  
Xenopus Laevis Oocytes ◽  
Xenopus Laevis Oocyte ◽  
U6 Snrna ◽  
Small Nuclear Ribonucleoprotein ◽  
La Protein ◽  
Shift Analysis

We have identified and characterized a U6 small nuclear (sn) ribonucleoprotein particle (RNP) present in the nuclei of Xenopus laevis oocytes. The structure of this U6 snRNP was investigated by native gel shift analysis and a combination of RNA-protein UV cross-linking, RNase T1 fingerprinting, and immunoprecipitation assays. These analyses demonstrate that certain forms of U6 snRNA associate with the 50-kDa nuclear antigen La both in vivo and in vitro. The La protein binds the stretch of uridylates at the 3' hydroxyl end of newly synthesized U6 snRNA. La does not bind to mature U6 snRNAs that have 2',3'-cyclic phosphate (greater than p) groups at their 3' ends (E. Lund and J. E. Dahlberg, Science 255:327-330, 1992) or to U6 snRNAs in anti-Sm-precipitable U4/U6 snRNPs. We propose that 3'-end modification, including posttranscriptional UMP addition, modulates the binding of La protein to U6 snRNA which, in turn, may affect the function of this RNA.

scholarly journals Accurate in vitro transcription of Xenopus laevis mitochondrial DNA from two bidirectional promoters.

1986 ◽  
Vol 6 (7) ◽  
pp. 2543-2550 ◽  
Author(s):  
D F Bogenhagen ◽  
B K Yoza
Keyword(s):  
Mitochondrial Dna ◽  
Xenopus Laevis ◽  
Rna Polymerase ◽  
Consensus Sequence ◽  
In Vitro Transcription ◽  
Xenopus Laevis Oocytes ◽  
Mitochondrial Rna ◽  
Bidirectional Promoters

The mitochondrial RNA polymerase from Xenopus laevis oocytes was partially purified by heparin-Sepharose chromatography and phosphocellulose chromatography. This RNA polymerase preparation specifically initiated the transcription of X. laevis mitochondrial DNA (mtDNA) from two bidirectional promoters contained within a 123-base-pair segment of the mtDNA between the heavy-strand replication origin and the rRNA cistrons. Transcription in vitro initiated from precisely the same start sites previously mapped as initiation sites for transcription in vivo. At each of the four sites, initiation occurred within a conserved nucleotide sequence, ACPuTTATA. This consensus sequence is not related to promoters for transcription of human mtDNA.

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