Uptake of Oocyte Nuclear Proteins by Nuclei of Xenopus Embryos

1986 ◽  
pp. 143-157 ◽  
Author(s):  
Chr. Dreyer ◽  
R. Stick ◽  
P. Hausen
Development ◽  
1987 ◽  
Vol 101 (4) ◽  
pp. 829-846 ◽  
Author(s):  
C. Dreyer

Oocyte nuclear proteins of Xenopus are distributed into the cytoplasm of the maturing egg after germinal vesicle breakdown. Later they are found in all cell nuclei of the embryo. At early stages of development, different nuclear proteins behave differently. A class of ‘early shifting’ antigens is accumulated by pronuclei and cleavage nuclei, whereas others appear to be excluded from the nuclei at early stages but are shifted into the nuclei at blastula or during and after gastrulation. Accumulation of ‘late-shifting’ nuclear antigens is a gradual process and occurs during a period characteristic of each protein. Multiple artificial pronuclei can be formed after injection of sperm nuclei, erythrocyte nuclei or pure lambda-DNA into unfertilized eggs. The artificial pronuclei accumulate early- but not late-shifting proteins. Early-migrating proteins rapidly accumulate into the germinal vesicle after de novo synthesis in the oocyte, indicating that the efficiency of translocation into nuclei is an intrinsic property of each protein. Artificial extension of the length of the cell cycle before midblastula transition does not lead to accumulation of the late-shifting nuclear antigens investigated.


Development ◽  
1987 ◽  
Vol 101 (4) ◽  
pp. 715-728
Author(s):  
C. Abbadie ◽  
D. Boucher ◽  
J. Charlemagne ◽  
J.C. Lacroix

The location of three proteins of the oocyte nucleus of Pleurodeles was studied during oogenesis and embryogenesis using monoclonal antibodies A33/22, C3/1 and C36/1. Immunoblotting of two-dimensional gel electrophoregrams of oocyte nuclear proteins showed that these antibodies recognized proteins whose relative molecular masses and isoelectric points were 80×103 and 6á4, 175×103 and 5 and 270×103 and 7, respectively. In the oocyte, all three proteins were nucleoplasmic; those revealed by antibodies A33/22 and C36/1 were detected on lampbrush chromosomes: the first one on the RNP matrix of the loops, and the second one on both the loops and the chromomeres. Protein A33/22 was observed in most nuclei during embryonic, larval and adult development, except for the young embryo, before the midblastula transition. The distribution of this protein in the oocyte and its behaviour during development suggest that it might be involved in the packaging of RNAs during transcription. Antibody C3/1 recognized an oocyte nucleoplasmic protein with biochemical and biophysical properties similar to those of protein N1-N2. After oocyte maturation, the protein moved into the cytoplasm of the animal hemisphere and, from fertilization to the midblastula stage, it shifted from the cytoplasm into the nuclei as cell division proceeded. Starting from the gastrula stage, this protein became specific to the endoderm nuclei. After hatching, it was no longer detectable. This behaviour seems to correspond to that of a nuclear protein issued from the maternal stock pile. Protein C36/1 behaved similarly during early development, but remained in most nuclei after neurulation until the adult age, with a pattern similar to that of protein A33/22. In addition, it was present on the mitotic chromosomes. Its association with mitotic as well as lampbrush chromosomes connects it with the DNP fibre proteins.


1982 ◽  
Vol 191 (4) ◽  
pp. 228-233 ◽  
Author(s):  
Christine Dreyer ◽  
Elke Scholz ◽  
Peter Hausen ◽  
Brigitte Gl�ser ◽  
Ursula M�ller ◽  
...  

Author(s):  
D.P. Bazett-Jones ◽  
F.P. Ottensmeyer

Dark field electron microscopy has been used for the study of the structure of individual macromolecules with a resolution to at least the 5Å level. The use of this technique has been extended to the investigation of structure of interacting molecules, particularly the interaction between DNA and fish protamine, a class of basic nuclear proteins of molecular weight 4,000 daltons.Protamine, which is synthesized during spermatogenesis, binds to chromatin, displaces the somatic histones and wraps up the DNA to fit into the small volume of the sperm head. It has been proposed that protamine, existing as an extended polypeptide, winds around the minor groove of the DNA double helix, with protamine's positively-charged arginines lining up with the negatively-charged phosphates of DNA. However, viewing protamine as an extended protein is inconsistent with the results obtained in our laboratory.


2013 ◽  
Vol 51 (01) ◽  
Author(s):  
C Hintemann ◽  
K Straub ◽  
S Biesterfeld ◽  
PR Galle ◽  
J Erthle ◽  
...  

1972 ◽  
Vol 71 (2_Suppla) ◽  
pp. S346-S368 ◽  
Author(s):  
Roger W. Turkington ◽  
Nobuyuki Kadohama

ABSTRACT Hormonal activation of gene transcription has been studied in a model system, the mouse mammary gland in organ culture. Transcriptive activity is stimulated in mammary stem cells by insulin, and in mammary alveolar cells by prolactin and insulin. Studies on the template requirement for expression of the genes for milk proteins demonstrate that DNA methylation has an obligatory dependence upon DNA synthesis, but is otherwise independent from hormonal regulation of mammary cell differentiation. Incorporation of 5-bromo-2′deoxyuridine into DNA selectively inhibits expression of the genes for specific milk proteins. Undifferentiated mammary cells activate the synthesis of specific acidic nuclear proteins when stimulated by insulin. Several of these induced acidic nuclear proteins are undetectable in unstimulated undifferentiated cells, but appear to be characteristic components of the nuclei of differentiated cells. These results indicate that mammary cell differentiation is associated with a change in acidic nuclear proteins, and they provide evidence to support the concept that acidic nuclear proteins may be involved in the regulation of gene transcription and of mammary cell differentiation.


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