Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 5 de 5
Filter
Add more filters










Database
Publication year range
1.
Z Evid Fortbild Qual Gesundhwes ; 118-119: 56-63, 2016 Dec.
Article in German | MEDLINE | ID: mdl-27987569

ABSTRACT

INTRODUCTION: In Germany, nursing education ends with a final written, oral and practical exam. In the federal state of Berlin, Germany, all nursing students take centrally standardized written exams, while the practical and oral exams are developed by each individual nursing school or university and conducted without standardized protocols (non-central). Comparability might be seriously limited by this procedure. Since there is no official statistics available, the objective of this study is to compare the results of the final written, oral and practical exams of different nursing education institutions with an additional focus on different educational concepts. METHODS: In a secondary data analysis, the final grades (written, oral, practical) of 4,342 nursing students in all 16 educational institutions in Berlin from 2008 to 2013 were analyzed. RESULTS: The mean (SD) of all written, oral and practical exams taken was 2.9 (0.7), 2.6 (1.1) and 2.2 (1.0), respectively. In each type of exam, the trend in grades was stable over the observation period. There was a statistically significant increase in the prevalence of initially failed exams from 2008 (7.9 %) to 2013 (12.0 %). In institutions following a traditional concept of education, the difference in grades between oral/practical exams on the one hand and written exams on the other ranged from 0.1 to 0.9, while in generalist (academic) institutions it ranged between -0.1 and 0.3 (-0.1 to 0). CONCLUSION: In nursing schools with a traditional approach to education, there was a big difference in grades between written and oral/practical exams. Standardization of oral and practical exams should be initiated to ensure greater comparability between different educational institutions.


Subject(s)
Education, Nursing , Educational Measurement , Berlin , Humans
2.
Epigenetics Chromatin ; 4: 11, 2011 Jul 20.
Article in English | MEDLINE | ID: mdl-21774791

ABSTRACT

BACKGROUND: Covalent histone modifications are central to all DNA-dependent processes. Modifications of histones H3 and H4 are becoming well characterised, but knowledge of how H2A modifications regulate chromatin dynamics and gene expression is still very limited. RESULTS: To understand the function of H2A modifications, we performed a systematic analysis of the histone H2A methylation status. We identified and functionally characterised two new methylation sites in H2A: R11 (H2AR11) and R29 (H2AR29). Using an unbiased biochemical approach in combination with candidate assays we showed that protein arginine methyltransferase (PRMT) 1 and PRMT6 are unique in their ability to catalyse these modifications. Importantly we found that H2AR29me2 is specifically enriched at genes repressed by PRMT6, implicating H2AR29me2 in transcriptional repression. CONCLUSIONS: Our data establishes R11 and R29 as new arginine methylation sites in H2A. We identified the specific modifying enzymes involved, and uncovered a novel functional role of H2AR29me2 in gene silencing in vivo. Thus this work reveals novel insights into the function of H2A methylation and in the mechanisms of PRMT6-mediated transcriptional repression.

3.
PLoS Genet ; 6(12): e1001234, 2010 Dec 09.
Article in English | MEDLINE | ID: mdl-21170357

ABSTRACT

The tails of histone proteins are central players for all chromatin-mediated processes. Whereas the N-terminal histone tails have been studied extensively, little is known about the function of the H2A C-terminus. Here, we show that the H2A C-terminal tail plays a pivotal role in regulating chromatin structure and dynamics. We find that cells expressing C-terminally truncated H2A show increased stress sensitivity. Moreover, both the complete and the partial deletion of the tail result in increased histone exchange kinetics and nucleosome mobility in vivo and in vitro. Importantly, our experiments reveal that the H2A C-terminus is required for efficient nucleosome translocation by ISWI-type chromatin remodelers and acts as a novel recognition module for linker histone H1. Thus, we suggest that the H2A C-terminal tail has a bipartite function: stabilisation of the nucleosomal core particle, as well as mediation of the protein interactions that control chromatin dynamics and conformation.


Subject(s)
Chromatin Assembly and Disassembly , Chromatin/metabolism , Histones/chemistry , Histones/metabolism , Amino Acid Motifs , Cell Line , Chromatin/genetics , Histones/genetics , Humans , Nucleosomes/genetics , Nucleosomes/metabolism , Protein Binding
4.
J Cell Sci ; 122(Pt 14): 2402-12, 2009 Jul 15.
Article in English | MEDLINE | ID: mdl-19531588

ABSTRACT

The a2 mating-type-locus gene lga2 of the basidiomycete Ustilago maydis encodes a mitochondrial protein that interferes with mitochondrial morphology and integrity, and that plays a role in uniparental inheritance of mitochondrial DNA. To address the mode of action of Lga2, we investigated its Dnm1 (a dynamin-related protein)-dependent effects. Here, we demonstrate that Dnm1 functions as a mitochondrial fission component in U. maydis and mediates Lga2-induced mitochondrial fragmentation. Mitochondrial fusion occurred very inefficiently in matings of U. maydis wild-type strains, but was strongly stimulated in the absence of dnm1 and highest in either wild-type or Deltadnm1 combinations when the a2 partner was deleted in lga2. This indicates that Dnm1 plays a central role in opposing mitochondrial fusion in response to endogenous lga2 expression and that Lga2 additionally inhibits fusion in a dnm1-independent manner. Our results further show that Lga2 does not stimulate increased turnover of the putative fusion protein Fzo1 and causes mitochondrial branching, loss of mitochondrial DNA and fitness reduction independently of dnm1. We conclude that Lga2 acts upstream of Dnm1, but controls mitochondrial integrity independently of Dnm1-mediated fission. In addition, we demonstrate a role of dnm1 in fungal virulence.


Subject(s)
Cytoskeletal Proteins/metabolism , Fungal Proteins/metabolism , Genes, Mating Type, Fungal , Membrane Fusion , Mitochondria/metabolism , Mitochondrial Proteins/metabolism , Ustilago/metabolism , Cell Division , Cytoskeletal Proteins/genetics , DNA, Mitochondrial/metabolism , Fungal Proteins/genetics , Gene Expression Regulation, Fungal , Membrane Fusion/genetics , Mitochondrial Proteins/genetics , Mutation , Time Factors , Ustilago/genetics , Ustilago/growth & development , Ustilago/pathogenicity , Virulence
5.
Nat Cell Biol ; 9(3): 347-53, 2007 Mar.
Article in English | MEDLINE | ID: mdl-17277772

ABSTRACT

Posttranslational modifications of histones, such as methylation, regulate chromatin structure and gene expression. Recently, lysine-specific demethylase 1 (LSD1), the first histone demethylase, was identified. LSD1 interacts with the androgen receptor and promotes androgen-dependent transcription of target genes by ligand-induced demethylation of mono- and dimethylated histone H3 at Lys 9 (H3K9) only. Here, we identify the Jumonji C (JMJC) domain-containing protein JMJD2C as the first histone tridemethylase regulating androgen receptor function. JMJD2C interacts with androgen receptor in vitro and in vivo. Assembly of ligand-bound androgen receptor and JMJD2C on androgen receptor-target genes results in demethylation of trimethyl H3K9 and in stimulation of androgen receptor-dependent transcription. Conversely, knockdown of JMJD2C inhibits androgen-induced removal of trimethyl H3K9, transcriptional activation and tumour cell proliferation. Importantly, JMJD2C colocalizes with androgen receptor and LSD1 in normal prostate and in prostate carcinomas. JMJD2C and LSD1 interact and both demethylases cooperatively stimulate androgen receptor-dependent gene transcription. In addition, androgen receptor, JMJD2C and LSD1 assemble on chromatin to remove methyl groups from mono, di and trimethylated H3K9. Thus, our data suggest that specific gene regulation requires the assembly and coordinate action of demethylases with distinct substrate specificities.


Subject(s)
Neoplasm Proteins/metabolism , Oxidoreductases, N-Demethylating/metabolism , Receptors, Androgen/metabolism , Transcription Factors/metabolism , Animals , Cell Line , Cell Line, Tumor , Cell Proliferation/drug effects , Chlorocebus aethiops , Gene Expression Regulation/drug effects , HeLa Cells , Histone Demethylases , Histones/metabolism , Humans , Jumonji Domain-Containing Histone Demethylases , Male , Metribolone/pharmacology , MicroRNAs/genetics , Neoplasm Proteins/genetics , Oxidoreductases, N-Demethylating/genetics , Prostate-Specific Antigen/genetics , Prostate-Specific Antigen/metabolism , Prostatic Neoplasms/genetics , Prostatic Neoplasms/metabolism , Prostatic Neoplasms/pathology , Protein Binding/drug effects , RNA, Small Interfering/genetics , Receptors, Androgen/analysis , Receptors, Glucocorticoid/genetics , Receptors, Glucocorticoid/metabolism , Receptors, Progesterone/genetics , Receptors, Progesterone/metabolism , Response Elements/genetics , Tissue Kallikreins/genetics , Transcription Factors/genetics , Transfection
SELECTION OF CITATIONS
SEARCH DETAIL
...