CCL

Összesen 2 találat.
#/oldal:
Részletezés:
Rendezés:

1.

001-es BibID:BIBFORM049213
Első szerző:Brázda Péter (biológus, angol-magyar szakfordító)
Cím:Ligand binding shifts highly mobile RXR to chromatin-bound state in a coactivator-dependent manner as revealed by single cell imaging / Peter Brazda, Jan Krieger, Bence Daniel, David Jonas, Tibor Szekeres, Jörg Langowski, Katalin Tóth, Laszlo Nagy, György Vámosi
Dátum:2014
ISSN:0270-7306
Megjegyzések:Retinoid X Receptor (RXR) is a promiscuous nuclear receptor forming heterodimers with several other receptors, which activate different sets of genes. Upon agonist treatment the occupancy of its genomic binding regions increased, but only a modest change in the number of sites was revealed by ChIP-Seq, suggesting a rather static behavior. However, such genome-wide and biochemical approaches do not take into account the dynamic behavior of a transcription factor. Therefore we characterized the nuclear dynamics of RXR during activation in single cells on the sub-second scale using live-cell imaging. By applying FRAP and fluorescence correlation spectroscopy (FCS), techniques with different temporal and spatial resolution, a highly dynamic behavior could be uncovered, which is best described by a two-state model of receptor mobility. In the unliganded state most RXRs belonged to the fast population, leaving ~15% for the slow, chromatin bound fraction. Upon agonist treatment, this ratio increased to ~43% as a result of an immediate and reversible redistribution. Coactivator binding appears to be indispensable for redistribution and has a major contribution to chromatin association. A nuclear mobility map recorded by light sheet microscopy-FCS shows that the ligand-induced transition from the fast to the slow population occurs throughout the nucleus. Our results support a model in which RXR has a distinct, highly dynamic nuclear behavior and follows hit-and-run kinetics upon activation.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
RXR
dynamics
nuclear receptor
diffusion
transcription
Megjelenés:Molecular and Cellular Biology. - 34 : 7 (2014), p. 1234-1245. -
További szerzők:Krieger, Jan W. Dániel Bence (1987-) (molekuláris biológus) Jonás Dávid Szekeres Tibor (1984-) (molekuláris biológus) Langowski, Jörg Tóth Katalin Ágnes (1977-) (biokémikus, molekuláris biológus) Nagy László (1966-) (molekuláris sejtbiológus, biokémikus) Vámosi György (1967-) (biofizikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
DOI
Borító:

2.

001-es BibID:BIBFORM060655
Első szerző:Szalóki Nikoletta (biológus)
Cím:Evidence for Homodimerization of the c-Fos Transcription Factor in Live Cells Revealed by Fluorescence Microscopy and Computer Modeling / Nikoletta Szalóki, Jan Wolfgang Krieger, István Komáromi, Katalin Tóth, György Vámosi
Dátum:2015
ISSN:0270-7306
Megjegyzések:The c-Fos and c-Jun transcription factors, members of the activator protein 1 (AP-1) complex, form heterodimers and bind to DNA via a basic leucine zipper and regulate the cell cycle, apoptosis, differentiation, etc. Purified c-Jun leucine zipper fragments could also form stable homodimers, whereas c-Fos leucine zipper homodimers were found to be much less stable in earlier in vitro studies. The importance of c-Fos overexpression in tumors and the controversy in the literature concerning c-Fos homodimerization prompted us to investigate Fos homodimerization. Förster resonance energy transfer (FRET) and molecular brightness analysis of fluorescence correlation spectroscopy data from live HeLa cells transfected with fluorescent-protein-tagged c-Fos indicated that c-Fos formed homodimers. We developed a method to determine the absolute concentrations of transfected and endogenous c-Fos and c-Jun, which allowed us to determine dissociation constants of c-Fos homodimers (Kd = 6.7 ? 1.7 ?M) and c-Fos?c-Jun heterodimers (on the order of 10 to 100 nM) from FRET titrations. Imaging fluorescence cross-correlation spectroscopy (SPIM-FCCS) and molecular dynamics modeling confirmed that c-Fos homodimers were stably associated and could bind to the chromatin. Our results establish c-Fos homodimers as a novel form of the AP-1 complex that may be an autonomous transcription factor in c-Fos-overexpressing tissues and could contribute to tumor development.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
c-Fos
homodimerization
dissociation constant
fluorescence correlation spectroscopy
SPIM-FCCS
FRET
live cell imaging
oncogene
protein-protein interactions
protein-DNA interactions
Megjelenés:Molecular And Cellular Biology. - 35 : 21 (2015), p. 3785-3798. -
További szerzők:Krieger, Jan Wolfgang Komáromi István (1957-) (vegyész, molekuláris biológus, biokémikus) Tóth Katalin (Heidelberg) Vámosi György (1967-) (biofizikus)
Pályázati támogatás:K103965
OTKA
TÁMOP-4.2.2.A-11/1/KONV-2012-0023
TÁMOP
MÖB/21-1/2013
Egyéb
TÁMOP-4.2.4.A/2- 11/1-2012-0001
TÁMOP
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Rekordok letöltése1