TY  - JOUR
A1  - Gross, Henrik
A1  - Hennard, Christine
A1  - Masouris, Ilias
A1  - Cassel, Christian
A1  - Barth, Stephanie
A1  - Stober-Grässer, Ute
A1  - Mamiani, Alfredo
A1  - Moritz, Bodo
A1  - Ostareck, Dirk
A1  - Ostareck-Lederer, Antje
A1  - Neuenkirchen, Nils
A1  - Fischer, Utz
A1  - Deng, Wen
A1  - Leonhardt, Heinrich
A1  - Noessner, Elfriede
A1  - Kremmer, Elisabeth
A1  - Grässer, Friedrich A.
T1  - Binding of the Heterogeneous Ribonucleoprotein K (hnRNP K) to the Epstein-Barr Virus Nuclear Antigen 2 (EBNA2) Enhances Viral LMP2A Expression
JF  - PLoS One
N2  - The Epstein-Barr Virus (EBV) -encoded EBNA2 protein, which is essential for the in vitro transformation of B-lymphocytes, interferes with cellular processes by binding to proteins via conserved sequence motifs. Its Arginine-Glycine (RG) repeat element contains either symmetrically or asymmetrically di-methylated arginine residues (SDMA and ADMA, respectively). EBNA2 binds via its SDMA-modified RG-repeat to the survival motor neurons protein (SMN) and via the ADMA-RG-repeat to the NP9 protein of the human endogenous retrovirus K (HERV-K (HML-2) Type 1). The hypothesis of this work was that the methylated RG-repeat mimics an epitope shared with cellular proteins that is used for interaction with target structures. With monoclonal antibodies against the modified RG-repeat, we indeed identified cellular homologues that apparently have the same surface structure as methylated EBNA2. With the SDMA-specific antibodies, we precipitated the Sm protein D3 (SmD3) which, like EBNA2, binds via its SDMA-modified RG-repeat to SMN. With the ADMA-specific antibodies, we precipitated the heterogeneous ribonucleoprotein K (hnRNP K). Specific binding of the ADMA-antibody to hnRNP K was demonstrated using E. coli expressed/ADMA-methylated hnRNP K. In addition, we show that EBNA2 and hnRNP K form a complex in EBV-infected B-cells. Finally, hnRNP K, when co-expressed with EBNA2, strongly enhances viral latent membrane protein 2A (LMP2A) expression by an unknown mechanism as we did not detect a direct association of hnRNP K with DNA-bound EBNA2 in gel shift experiments. Our data support the notion that the methylated surface of EBNA2 mimics the surface structure of cellular proteins to interfere with or co-opt their functional properties.
KW  - SM proteins
KW  - protein argentine methyltranserase
KW  - motor-neuron protein
KW  - RNA-polymerase-II
KW  - messenger RNA
KW  - C-MYC
KW  - gene expression
KW  - splicing factor
KW  - down regulation
KW  - living cells
Y1  - 2012
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-133707
VL  - 7
IS  - 8
ER  - 
TY  - JOUR
A1  - Groß, Elisabeth
A1  - Burschka, Christian
A1  - Malisch, Wolfgang
T1  - Hauptgruppenelement-Übergangsmetall-Mehrfachbindungen, IV. Katalytische Assistenz von [Cp(C0)\(_3\)Mo]\(_2\) bei der Aggregation von Metallo-arsanen über Arsen-Metall-Doppelbindungskomplexe
T1  - Main Group Element Transition Metal Multiple Bonds, IV. Catalytic Assistance by [Cp(CO)\(_3\)Mo]\(_2\) in the Aggregation of Metalloarsines via Arsenic Metal Double Bond Complexes
N2  - The metallo-arsanes CP(CO)\(_3\)M - AsMc\(_2\) (1 a, b) (M = Mo, W) are convcrted to the double arsenido-bridged dinuclear complexes [(η-AsMe\(_2\))Mo(CO)\(_2\)Cp]\(_2\) (3a, b) in the presence of [CP(CO)\(_3\)Mo]\(_2\). Due to the unusual mild conditions of aggregation the intermediate formation of the double bonded species Cp(CO)\(_2\)M = AsMe\(_2\) (2a, b) is postulated. The crystal structure of 3a is reported, which shows mutual trans arrangement of the cyclopentadienyl and CO ligands.
KW  - Chemie
Y1  - 1986
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-31424
ER  - 
TY  - JOUR
A1  - Schümann, Franziska Lea
A1  - Groß, Elisabeth
A1  - Bauer, Marcus
A1  - Rohde, Christian
A1  - Sandmann, Sarah
A1  - Terziev, Denis
A1  - Müller, Lutz P.
A1  - Posern, Guido
A1  - Wienke, Andreas
A1  - Fend, Falko
A1  - Hansmann, Martin-Leo
A1  - Klapper, Wolfram
A1  - Rosenwald, Andreas
A1  - Stein, Harald
A1  - Dugas, Martin
A1  - Müller-Tidow, Carsten
A1  - Wickenhauser, Claudia
A1  - Binder, Mascha
A1  - Weber, Thomas
T1  - Divergent effects of EZH1 and EZH2 protein expression on the prognosis of patients with T-cell lymphomas
JF  - Biomedicines
N2  - T-cell lymphomas are highly heterogeneous and their prognosis is poor under the currently available therapies. Enhancers of zeste homologue 1 and 2 (EZH1/2) are histone H3 lysine-27 trimethyltransferases (H3K27me3). Despite the rapid development of new drugs inhibiting EZH2 and/or EZH1, the molecular interplay of these proteins and the impact on disease progression and prognosis of patients with T-cell lymphomas remains insufficiently understood. In this study, EZH1/2 mutation status was evaluated in 33 monomorphic epitheliotropic intestinal T-cell lymphomas by next generation sequencing and EZH1/2 and H3K27me3 protein expression levels were detected by immunohistochemistry in 46 T-cell lymphomas. Correlations with clinicopathologic features were analyzed and survival curves generated. No EZH1 mutations and one (3%) EZH2 missense mutation were identified. In univariable analysis, high EZH1 expression was associated with an improved overall survival (OS) and progression-free survival (PFS) whereas high EZH2 and H3K27me3 expression were associated with poorer OS and PFS. Multivariable analysis revealed EZH1 (hazard ratio (HR) = 0.183; 95% confidence interval (CI): 0.044–0.767; p = 0.020;) and EZH2 (HR = 8.245; 95% CI: 1.898–35.826; p = 0.005) to be independent, divergent prognostic markers for OS. In conclusion, EZH1/2 protein expression had opposing effects on the prognosis of T-cell lymphoma patients.
KW  - T-cell non-Hodgkin's lymphomas
KW  - PTCL
KW  - epigenetics
KW  - EZH1
KW  - EZH2
KW  - H3K27me3
KW  - immunohistochemistry
KW  - next generation sequencing
Y1  - 2021
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-252155
SN  - 2227-9059
VL  - 9
IS  - 12
ER  -