Protein Phosphorylation and Chromatin Replication: Studies on the Interaction of Two Nuclear Proteins with DNA

1983 ◽  
pp. 179-192
Author(s):  
Hans Stahl ◽  
Herbert König ◽  
Rolf Knippers
Keyword(s):  
Protein Phosphorylation ◽  
Nuclear Proteins ◽  
Replication Studies

scholarly journals Induction and properties of cytoplasmic factor(s) which enhance nuclear nonhistone protein phosphorylation in lymphocytes stimulated by anti-Ig.

1977 ◽  
Vol 146 (3) ◽  
pp. 653-664 ◽  
Author(s):  
Y Nishizawa ◽  
T Kishimoto ◽  
H Kikutani ◽  
Y Yamamura
Keyword(s):  
Protein Kinase ◽  
Protein Phosphorylation ◽  
Adenosine Triphosphate ◽  
Active Substance ◽  
Nuclear Proteins ◽  
Concomitant Increase ◽  
Cytoplasmic Factor ◽  
Nonhistone Protein ◽  
Rabbit Lymphocytes

An increased in vitro phosphorylation of nonhistone nuclear proteins (NHP) was observed in the nuclei isolated from rabbit lymphocytes which had been stimulated with anti-Ig for 4 h. No concomitant increase of phosphorylation in histones or 0.14 M NaCl-soluble proteins was observed. The increase of in vitro phosphorylation of NHP was also observed in the nuclei isolated from nonstimulated cells when these nuclei were preincubated for 2 h with cell-free extracts from anti-Ig-stimulated cells. The active substance in cell-free extracts was maximally induced when lymphocytes were stimulated with anti-Ig for 2 h. The induction of an increased phosphorylation of NHP in nonstimulated nuclei with the cell-free extracts was not due to decrease of the adenosine triphosphate pool in the extracts from anti-Ig-stimulated cells. The active substance in cell-free extracts was not NHP-protein kinase itself, but it probably activated NHP-protein kinase in quiescent nuclei. The active substance was nondialyzable and probably protein. It was resistant against heating at 56 degrees C for 30 min, but the activity was completely destroyed by heating at 90 degrees C for 30 min. The active substance may be responsible for the transduction of the membrane-mediated signals given through Ig receptors to nuclei.

scholarly journals Quantitative phosphoproteomic profiling of PINK1-deficient cells identifies phosphorylation changes in nuclear proteins

2014 ◽  
Vol 10 (7) ◽  
pp. 1719-1729 ◽  
Author(s):  
Xiaoyan Qin ◽  
Chaoya Zheng ◽  
John R. Yates III ◽  
Lujian Liao
Keyword(s):  
Parkinson’S Disease ◽  
Parkinson's Disease ◽  
Protein Phosphorylation ◽  
Nuclear Proteins

A quantitative phosphoproteomic method coupled with siRNA mediated silencing of a kinase associated with Parkinson's disease was applied to measure phosphorylation changes. The results indicate alterations in protein phosphorylation downstream of this kinase, potentially expanding our understanding of its function.

Holding replication studies to mainstream standards of evidence

2018 ◽  
Vol 41 ◽  
Author(s):  
Duane T. Wegener ◽  
Leandre R. Fabrigar
Keyword(s):  
Replication Studies ◽  
Replication Research ◽  
Standards Of Evidence ◽  
Do So

AbstractReplications can make theoretical contributions, but are unlikely to do so if their findings are open to multiple interpretations (especially violations of psychometric invariance). Thus, just as studies demonstrating novel effects are often expected to empirically evaluate competing explanations, replications should be held to similar standards. Unfortunately, this is rarely done, thereby undermining the value of replication research.

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.

Replication of Experiments Evaluating Impact of Psychological Distance on Moral Judgment

2014 ◽  
Vol 45 (3) ◽  
pp. 223-231 ◽  
Author(s):  
Iris L. Žeželj ◽  
Biljana R. Jokić
Keyword(s):  
Moral Judgment ◽  
Social Distance ◽  
Psychological Distance ◽  
Temporal Distance ◽  
Construal Level ◽  
Systematic Effect ◽  
Replication Studies ◽  
Opposite Conclusion ◽  
Moral Transgressions ◽  
Replication Of Experiments

Eyal, Liberman, and Trope (2008) established that people judged moral transgressions more harshly and virtuous acts more positively when the acts were psychologically distant than close. In a series of conceptual and direct replications, Gong and Medin (2012) came to the opposite conclusion. Attempting to resolve these inconsistencies, we conducted four high-powered replication studies in which we varied temporal distance (Studies 1 and 3), social distance (Study 2) or construal level (Study 4), and registered their impact on moral judgment. We found no systematic effect of temporal distance, the effect of social distance consistent with Eyal et al., and the reversed effect of direct construal level manipulation, consistent with Gong and Medin. Possible explanations for the incompatible results are discussed.

Involvement of protein phosphorylation in the sensitivity of photosystem II to strong illumination

1994 ◽  
Vol 92 (1) ◽  
pp. 181-187
Author(s):  
Maria T. Giardi ◽  
Josef Komenda ◽  
Jiri Masojidek
Keyword(s):  
Photosystem Ii ◽  
Protein Phosphorylation

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.

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