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001-es BibID:	BIBFORM054070
Első szerző:	Fuxreiter Mónika (kutató vegyész)
Cím:	Disordered Proteinaceous Machines / Monika Fuxreiter, Ágnes Tóth-Petróczy, Daniel A. Kraut, Andreas T. Matouschek, Roderick Y. H. Lim, Bin Xue, Lukasz Kurgan, Vladimir N. Uversky
Dátum:	2014
ISSN:	0009-2665
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Chemical Reviews. - 114 : 13 (2014), p. 6806-6843. -
További szerzők:	Tóth-Petróczy Ágnes Kraut, Daniel A. Matouschek, Andreas T. Lim, Roderick Y. H. Xue, Bin Kurgan, Lukasz Uversky, Vladimir N.
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001-es BibID:	BIBFORM031427
035-os BibID:	PMID:19919153 WOS:000271272000005
Első szerző:	Tóth-Petróczy Ágnes
Cím:	Disordered tails of homeodomains facilitate DNA recognition by providing a trade-off between folding and specific binding / Ágnes Tóth-Petróczy, Istvan Simon, Monika Fuxreiter, Yaakov Levy
Dátum:	2009
ISSN:	0002-7863
Megjegyzések:	DNA binding specificity of homeodomain transcription factors is critically affected by disordered N-terminal tails (N-tails) that undergo a disorder-to-order transition upon interacting with DNA. The mechanism of the binding process and the molecular basis of selectivity are largely unknown. The coupling between folding and DNA binding of Antp and NK-2 homeodomains was investigated by coarse-grained molecular dynamics simulations using the native protein-DNA complex. The disordered N-tails were found to decrease the stability of the free proteins by competing with the native intramolecular interactions and increasing the radius of gyration of the homeodomain cores. In the presence of DNA, however, the N-tails increase the stability of the homeodomains by reducing the coupling between folding and DNA binding. Detailed studies on Antp demonstrate that the N-tail anchors the homeodomain to DNA and accelerates formation of specific interactions all along the protein-DNA interface. The tidal electrostatic forces between the N-tail and DNA induce faster and tighter binding of the homeodomain core to the DNA; this mechanism conforms to a fly-casting mechanism. In agreement with experiments, the N-tail of Antp also improves the binding affinity for DNA, with a major contribution by the released waters. These results imply that varying the degree of folding upon binding and thereby modulating the size of the buried surface-disordered N-tails of homeodomains can fine-tune the binding strength for specific DNA sequences. Overall, both the kinetics and thermodynamics of specific DNA binding by homeodomains can be improved by N-tails using a mechanism that is inherent in their disordered state.
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban külföldön készült közlemény
Megjelenés:	Journal of the American Chemical Society. - 131 : 42 (2009), p. 15084-15085. -
További szerzők:	Simon István Fuxreiter Mónika (1969-) (kutató vegyész) Levy, Yaakov
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001-es BibID:	BIBFORM031420
035-os BibID:	WOS:000263923800012
Első szerző:	Tóth-Petróczy Ágnes
Cím:	Malleable machines in transcription regulation : the mediator complex / Ágnes Tóth-Petróczy, Christopher J. Oldfield, István Simon, Yuichiro Takagi, A. Keith Dunker, Vladimir N. Uversky, Mónika Fuxreiter
Dátum:	2008
ISSN:	1553-734X
Megjegyzések:	The Mediator complex provides an interface between gene-specific regulatory proteins and the general transcription machinery including RNA polymerase II (RNAP II). The complex has a modular architecture (Head, Middle, and Tail) and cryoelectron microscopy analysis suggested that it undergoes dramatic conformational changes upon interactions with activators and RNAP II. These rearrangements have been proposed to play a role in the assembly of the preinitiation complex and also to contribute to the regulatory mechanism of Mediator. In analogy to many regulatory and transcriptional proteins, we reasoned that Mediator might also utilize intrinsically disordered regions (IDRs) to facilitate structural transitions and transmit transcriptional signals. Indeed, a high prevalence of IDRs was found in various subunits of Mediator from both Saccharomyces cerevisiae and Homo sapiens, especially in the Tail and the Middle modules. The level of disorder increases from yeast to man, although in both organisms it significantly exceeds that of multiprotein complexes of a similar size. IDRs can contribute to Mediator's function in three different ways: they can individually serve as target sites for multiple partners having distinctive structures; they can act as malleable linkers connecting globular domains that impart modular functionality on the complex; and they can also facilitate assembly and disassembly of complexes in response to regulatory signals. Short segments of IDRs, termed molecular recognition features (MoRFs) distinguished by a high protein-protein interaction propensity, were identified in 16 and 19 subunits of the yeast and human Mediator, respectively. In Saccharomyces cerevisiae, the functional roles of 11 MoRFs have been experimentally verified, and those in the Med8/Med18/Med20 and Med7/Med21 complexes were structurally confirmed. Although the Saccharomyces cerevisiae and Homo sapiens Mediator sequences are only weakly conserved, the arrangements of the disordered regions and their embedded interaction sites are quite similar in the two organisms. All of these data suggest an integral role for intrinsic disorder in Mediator's function.
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban egyetemen (Magyarországon) készült közlemény
Megjelenés:	PLoS Computational Biology. - 4 : 12 (2008), p. e1000243. -
További szerzők:	Oldfield, Christopher J. Simon István Takagi, Yuichiro Dunker, A. Keith Uversky, Vladimir N. Fuxreiter Mónika (1969-) (kutató vegyész)
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001-es BibID:	BIBFORM031416
Első szerző:	Tóth-Petróczy Ágnes
Cím:	Assessing conservation of disordered regions in proteins / Ágnes Tóth-Petróczy, Bálint Mészáros, István Simon, A. Keith Dunker, Vladimir N. Uversky, Monika Fuxreiter
Dátum:	2008
ISSN:	1875-0397
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban egyetemen (Magyarországon) készült közlemény
Megjelenés:	Open Proteomics Journal. - 1 : 1 (2008), p. 46-53. -
További szerzők:	Mészáros Bálint Simon István Dunker, A. Keith Uversky, Vladimir N. Fuxreiter Mónika (1969-) (kutató vegyész)
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat
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