Oligomerization and DNA-Binding Capacity of Pmr, a Histone-Like Protein H1 (H-NS) Family Protein Encoded on IncP-7 Carbazole-Degradative Plasmid pCAR1

2011 ◽  
Vol 75 (4) ◽  
pp. 711-717 ◽  
Author(s):  
Chiho SUZUKI ◽  
Choong-Soo YUN ◽  
Takashi UMEDA ◽  
Tsuguno TERABAYASHI ◽  
Kazuya WATANABE ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Capacity ◽  
Family Protein ◽  
Degradative Plasmid

scholarly journals Intranuclear Crosstalk between Extracellular Regulated Kinase1/2 and Signal Transducer and Activator of Transcription 3 Regulates JEG-3 Choriocarcinoma Cell Invasion and Proliferation

2013 ◽  
Vol 2013 ◽  
pp. 1-10 ◽  
Author(s):  
Diana M. Morales-Prieto ◽  
Stephanie Ospina-Prieto ◽  
Wittaya Chaiwangyen ◽  
Maja Weber ◽  
Sebastian Hölters ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Capacity ◽  
Mapk Signaling ◽  
Signaling Molecules ◽  
Signal Transducer ◽  
Stat3 Phosphorylation ◽  
Functional Implications ◽  
Choriocarcinoma Cells ◽  
Cell Invasiveness ◽  
Transcription 3

Invasiveness of trophoblast and choriocarcinoma cells is in part mediated via leukemia inhibitory factor- (LIF-) induced activation of signal transducer and activator of transcription 3 (STAT3). The regulation of STAT3 phosphorylation at its ser727 binding site, possible crosstalk with intracellular MAPK signaling, and their functional implications are the object of the present investigation. JEG-3 choriocarcinoma cells were cultured in presence/absence of LIF and the specific ERK1/2 inhibitor (U0126). Phosphorylation of signaling molecules (p-STAT3 (ser727 and tyr705) and p-ERK1/2 (thr 202/tyr 204)) was assessed per Western blot. Immunocytochemistry confirmed results, but also pinpointed the location of phosphorylated signaling molecules. STAT3 DNA-binding capacity was studied with a colorimetric ELISA-based assay. Cell viability and invasion capability were assessed by MTS and Matrigel assays. Our results demonstrate that LIF-induced phosphorylation of STAT3 (tyr705 and ser727) is significantly increased after blocking ERK1/2. STAT3 DNA-binding capacity and cell invasiveness are enhanced after LIF stimulation and ERK1/2 blockage. In contrast, proliferation is enhanced by LIF but reduced after ERK1/2 inhibition. The findings herein show that blocking ERK1/2 increases LIF-induced STAT3 phosphorylation and STAT3 DNA-binding capacity by an intranuclear crosstalk, which leads to enhanced invasiveness and reduced proliferation.

scholarly journals polA6, a mutation affecting the DNA binding capacity of DNA polymerase I

1976 ◽  
Vol 3 (11) ◽  
pp. 2971-2984 ◽  
Author(s):  
W. S. Kelly ◽  
N. D. F. Grindley
Keyword(s):  
Dna Binding ◽  
Dna Polymerase ◽  
Binding Capacity ◽  
Dna Polymerase I ◽  
Polymerase I

scholarly journals Structural basis for osmotic regulation of the DNA binding properties of H-NS proteins

2019 ◽  
Author(s):  
Liang Qin ◽  
Fredj Ben Bdira ◽  
Yann G. J. Sterckx ◽  
Alexander N. Volkov ◽  
Jocelyne Vreede ◽  
...  
Keyword(s):  
Dna Binding ◽  
Electrostatic Interactions ◽  
Intramolecular Interactions ◽  
Structural Basis ◽  
Binding Properties ◽  
Family Protein ◽  
Low Salt ◽  
Functional States ◽  
Mechanistic Basis ◽  
Dna Binding Properties

AbstractH-NS proteins act as osmotic sensors translating changes in osmolarity into altered DNA binding properties, thus, regulating enterobacterial genome organization and genes transcription. The molecular mechanism underlying the switching process and its conservation among H-NS family members remains elusive.Here, we focus on the H-NS family protein MvaT from P. aeruginosa and demonstrate experimentally that its protomer exists in two different conformations, corresponding to two different functional states. In the half-opened state (dominant at low salt) the protein forms filaments along DNA, in the fully opened state (dominant at high salt) the protein bridges DNA. This switching is a direct effect of ionic strengths on electrostatic interactions between the appositively charged DNA binding and N-terminal domains of MvaT. The asymmetric charge distribution and intramolecular interactions are conserved among the H-NS family of proteins. Therefore, our study establishes a general paradigm for the molecular mechanistic basis of the osmosensitivity of H-NS proteins.

scholarly journals Mitosis-specific phosphorylation of the nuclear oncoproteins Myc and Myb.

1992 ◽  
Vol 118 (4) ◽  
pp. 775-784 ◽  
Author(s):  
B Lüscher ◽  
R N Eisenman
Keyword(s):  
Transcriptional Regulation ◽  
Dna Binding ◽  
Nuclear Dna ◽  
Binding Capacity ◽  
Dna Binding Proteins ◽  
Response Element ◽  
Double Stranded Dna ◽  
M Phase ◽  
Myb Proteins

The c-myc and c-myb proto-oncogenes encode phosphorylated nuclear DNA binding proteins that are likely to be involved in transcriptional regulation. Here we demonstrate that both Myc and Myb proteins are hyperphosphorylated during mitosis. In the case of Myb, hyperphosphorylation is accompanied by the appearance of three M phase-specific tryptic phosphopeptides. At least one of these phosphopeptides corresponds to a phosphopeptide generated after phosphorylation of Myb in vitro by p34cdc2 kinase. By contrast, the mitotic hyperphosphorylation of Myc does not correlate with the appearance of unique phosphopeptides, suggesting that M phase and interphase sites may be clustered within the same peptides. In addition Myc does not appear to be a target for p34cdc2 phosphorylation. The hyperphosphorylated forms of Myc and Myb from mitotic cells are functionally distinct from the corresponding interphase proteins in that the former have reduced ability to bind nonspecificially to double-stranded DNA cellulose. Furthermore, mitotic Myb binds poorly to oligodeoxynucleotides containing an Myb response element. We surmise that the decreased DNA binding capacity of hyperphosphorylated Myb and Myc during M phase may function to release these proteins from chromatin during chromosome condensation.

Oncostatin M and leukaemia inhibitory factor trigger signal transducer and activator of transcription 3 and extracellular signal-regulated kinase 1/2 pathways but result in heterogeneous cellular responses in trophoblast cells

2016 ◽  
Vol 28 (5) ◽  
pp. 608 ◽  
Author(s):  
Wittaya Chaiwangyen ◽  
Stephanie Ospina-Prieto ◽  
Diana M. Morales-Prieto ◽  
Francisco Lazaro Pereira de Sousa ◽  
Jana Pastuschek ◽  
...  
Keyword(s):  
Dna Binding ◽  
Cell Lines ◽  
Binding Capacity ◽  
Binding Activity ◽  
Oncostatin M ◽  
Inhibitory Factor ◽  
Therapeutic Interventions ◽  
Leukaemia Inhibitory Factor ◽  
Tetrazolium Salt ◽  
Signal Transducer

Leukaemia inhibitory factor (LIF) and oncostatin M (OSM) are pleiotropic cytokines present at the implantation site that are important for the normal development of human pregnancy. These cytokines share the cell membrane receptor subunit gp130, resulting in similar functions. The aim of this study was to compare the response to LIF and OSM in several trophoblast models with particular regard to intracellular mechanisms and invasion. Four trophoblast cell lines with different characteristics were used: HTR-8/SVneo, JEG-3, ACH-3P and AC1-M59 cells. Cells were incubated with LIF, OSM (both at 10 ng mL–1) and the signal transducer and activator of transcription (STAT) 3 inhibitor S3I-201 (200 µM). Expression and phosphorylation of STAT3 (tyr705) and extracellular regulated kinase (ERK) 1/2 (thr202/204) and the STAT3 DNA-binding capacity were analysed by Western blotting and DNA-binding assays, respectively. Cell viability and invasiveness were assessed by the methylthiazole tetrazolium salt (MTS) and Matrigel assays. Enzymatic activity of matrix metalloproteinase (MMP)-2 and MMP-9 was investigated by zymography. OSM and LIF triggered phosphorylation of STAT3 and ERK1/2, followed by a significant increase in STAT3 DNA-binding activity in all tested cell lines. Stimulation with LIF but not OSM significantly enhanced invasion of ACH-3P and JEG-3 cells, but not HTR-8/SVneo or AC1-M59 cells. Similarly, STAT3 inhibition significantly decreased the invasiveness of only ACH-3P and JEG-3 cells concomitant with decreases in secreted MMP-2 and MMP-9. OSM shares with LIF the capacity to activate ERK1/2 and STAT3 pathways in all cell lines tested, but their resulting effects are dependent on cell type. This suggests that LIF and OSM may partially substitute for each other in case of deficiencies or therapeutic interventions.

Enhanced DNA binding capacity on up‐regulated epidermal wild‐type p53 in vitiligo by H 2 O 2 ‐mediated oxidation: a possible repair mechanism for DNA damage

2009 ◽  
Vol 23 (11) ◽  
pp. 3790-3807 ◽  
Author(s):  
Mohamed M. A. E. L. Salem ◽  
Mohammad Shalbaf ◽  
Nicholas C. J. Gibbons ◽  
Bhaven Chavan ◽  
J. M. Thornton ◽  
...  
Keyword(s):  
Dna Damage ◽  
Dna Binding ◽  
Binding Capacity ◽  
Wild Type ◽  
Repair Mechanism ◽  
Wild Type P53 ◽  
Mediated Oxidation

Cyclin D1/cdk4 can interact with E2F4/DP1 and disrupts its DNA-binding capacity

2007 ◽  
Vol 214 (3) ◽  
pp. 568-581 ◽  
Author(s):  
Anthony Scimè ◽  
Lili Li ◽  
Gianni Ciavarra ◽  
Peter Whyte
Keyword(s):  
Dna Binding ◽  
Cyclin D1 ◽  
Binding Capacity

scholarly journals Purification, Cloning, and Preliminary Characterization of aSpiroplasma citriRibosomal Protein with DNA Binding Capacity

1998 ◽  
Vol 273 (38) ◽  
pp. 24379-24386 ◽  
Author(s):  
Loı̈ck Le Dantec ◽  
Michel Castroviejo ◽  
Joseph M. Bové ◽  
Colette Saillard
Keyword(s):  
Dna Binding ◽  
Binding Capacity ◽  
Preliminary Characterization
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