Immunofluorescence Localization of Nuclear Proteins

2011 ◽  
Vol 2011 (10) ◽  
pp. pdb.prot065755-pdb.prot065755 ◽  
Author(s):  
D. L. Spector
Keyword(s):  
Nuclear Proteins ◽  
Immunofluorescence Localization

scholarly journals The yeast RNA1 gene product necessary for RNA processing is located in the cytosol and apparently excluded from the nucleus.

1990 ◽  
Vol 111 (2) ◽  
pp. 309-321 ◽  
Author(s):  
A K Hopper ◽  
H M Traglia ◽  
R W Dunst
Keyword(s):  
Gene Product ◽  
Indirect Immunofluorescence ◽  
Rna Processing ◽  
Nuclear Transport ◽  
Stress Conditions ◽  
Nuclear Proteins ◽  
Intracellular Location ◽  
Trna Splicing ◽  
Immunofluorescence Localization ◽  
Endogenous Protein

The yeast RNA1 gene is required for RNA processing and nuclear transport of RNA. The rna1-1 mutation of this locus causes defects in pre-tRNA splicing, processing of the primary pre-rRNA transcript, production of mRNA and export of RNA from the nucleus to the cytosol. To understand how this gene product can pleiotropically affect these processes, we sought to determine the intracellular location of the RNA1 protein. As determined by indirect immunofluorescence localization and organelle fractionation, the RNA1 antigen is found exclusively or primarily in the cytoplasm. Only a tiny fraction of the endogenous protein could be localized to and functional in the nucleus. Furthermore, the RNA1 antigen does not localize differently under stress conditions. These findings suggest that the RNA1 protein is not directly involved in RNA processing but may modify nuclear proteins or otherwise transmit a signal from the cytosol to the nucleus or play a role in maintaining the integrity of the nucleus.

Protamine-DNA interaction

1978 ◽  
Vol 36 (2) ◽  
pp. 200-201
Author(s):  
D.P. Bazett-Jones ◽  
F.P. Ottensmeyer
Keyword(s):  
Small Volume ◽  
Double Helix ◽  
Dna Interaction ◽  
Dark Field ◽  
Sperm Head ◽  
Nuclear Proteins ◽  
Field Electron Microscopy ◽  
Dark Field Electron ◽  
Dna Double Helix ◽  
Positively Charged

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.

Nuclear proteins in primary biliary cirrhosis as guardians against HCC development

2013 ◽  
Vol 51 (01) ◽  
Author(s):  
C Hintemann ◽  
K Straub ◽  
S Biesterfeld ◽  
PR Galle ◽  
J Erthle ◽  
...  
Keyword(s):  
Primary Biliary Cirrhosis ◽  
Nuclear Proteins ◽  
Biliary Cirrhosis

GENE ACTIVATION IN MAMMARY CELLS

1972 ◽  
Vol 71 (2_Suppla) ◽  
pp. S346-S368 ◽  
Author(s):  
Roger W. Turkington ◽  
Nobuyuki Kadohama
Keyword(s):  
Cell Differentiation ◽  
Gene Transcription ◽  
Hormonal Regulation ◽  
Gene Activation ◽  
Milk Proteins ◽  
Mouse Mammary Gland ◽  
Nuclear Proteins ◽  
Mammary Cells ◽  
Alveolar Cells ◽  
Mammary Cell

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.

Identification of Nuclear Proteins in Soybean Under Flooding Stress using Proteomic Technique

2014 ◽  
Vol 21 (5) ◽  
pp. 458-467 ◽  
Author(s):  
Myeong Oh ◽  
Yohei Nanjo ◽  
Setsuko Komatsu
Keyword(s):  
Nuclear Proteins ◽  
Flooding Stress

Outfielders Playing in the Infield: Functions of Aging-Associated "Nuclear" Proteins in the Mitochondria

2014 ◽  
Vol 14 (10) ◽  
pp. 1247-1251 ◽  
Author(s):  
P. Czypiorski ◽  
J. Altschmied ◽  
L.L. Rabanter ◽  
C. Goy ◽  
S. Jakob. ◽  
...  
Keyword(s):  
Nuclear Proteins

scholarly journals Tissue-specific interactions between nuclear proteins and the aminopeptidase N promoter.

1991 ◽  
Vol 266 (27) ◽  
pp. 18089-18096
Author(s):  
J. Olsen ◽  
L. Laustsen ◽  
U. Kärnström ◽  
H. Sjöström ◽  
O. Norén
Keyword(s):  
Aminopeptidase N ◽  
Nuclear Proteins ◽  
Specific Interactions ◽  
Tissue Specific
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