Dynamics and metal exchange properties of C4C4 RING domains from CNOT4 and the p44 subunit of TFIIH

Autor: Houben, Klaartje, Wasielewski, Emeric, Dominguez, Cyril, Kellenberger, Esther, Atkinson, R. Andrew, Timmers, H. Th. Marc, Kieffer, Bruno, Boelens, Rolf, Sub NMR Spectroscopy, NMR Spectroscopy
Přispěvatelé: Institut Gilbert-Laustriat : Biomolécules, Biotechnologie, Innovation Thérapeutique, Université Louis Pasteur - Strasbourg I-Centre National de la Recherche Scientifique (CNRS), Sub NMR Spectroscopy, NMR Spectroscopy, Klotz, Evelyne
Jazyk: angličtina
Rok vydání: 2005
Předmět:
NMR15N relaxation
Magnetic Resonance Spectroscopy
Molecular model
MESH: Amino Acid Sequence
ion exchange
01 natural sciences
MESH: Zinc
Transcription Factors
TFII
MESH: Protein Structure
Tertiary
Protein structure
Spectral density mapping
Structural Biology
Zinc finger
electricity
transcription factor
0303 health sciences
Ion exchange
MESH: Kinetics
MESH: Transcription Factor TFIIH
protein p44
article
protein domain
MESH: Transcription Factors
unclassified drug
Zinc
zinc ion
priority journal
protein stability
protein protein interaction
RING domain
Heteronuclear single quantum coherence spectroscopy
MESH: Nitrogen Isotopes
zinc finger protein
Metal exchange kinetics
cadmium
ccr4 not transcription complex subunit 4 protein
Molecular Sequence Data
Protein domain
MESH: Cadmium
chemistry.chemical_element
010402 general chemistry
Protein–protein interaction
03 medical and health sciences
MESH: Transcription Factors
TFII
physical chemistry
transcription factor IIH
Amino Acid Sequence
Molecular Biology
030304 developmental biology
nuclear magnetic resonance spectroscopy
MESH: Molecular Sequence Data
Nitrogen Isotopes
MESH: Magnetic Resonance Spectroscopy
binding site
metal binding
[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Molecular biology
protein subunit
molecular dynamics
Protein Structure
Tertiary
0104 chemical sciences
Kinetics
Crystallography
chemistry
molecular model
Transcription Factor TFIIH
Transcription Factors
Zdroj: Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2005, 349, pp.621-637
Journal of Molecular Biology, 349(3), 621. Academic Press Inc.
Journal of Molecular Biology, Elsevier, 2005, 349 (3), pp.621-37. ⟨10.1016/j.jmb.2005.04.007⟩
ISSN: 0022-2836
1089-8638
DOI: 10.1016/j.jmb.2005.04.007⟩
Popis: Zinc fingers are small structured protein domains that require the coordination of zinc for a stable tertiary fold. Together with FYVE and PHD, the RING domain forms a distinct class of zinc-binding domains, where two zinc ions are ligated in a cross-braced manner, with the first and third pairs of ligands coordinating one zinc ion, while the second and fourth pairs ligate the other zinc ion. To investigate the relationship between the stability and dynamic behaviour of the domains and the stability of the metal-binding site, we studied metal exchange for the C4C4 RING domains of CNOT4 and the p44 subunit of TFIIH. We found that Zn2+-Cd2+exchange is different between the two metal-binding sites in the C4C4 RING domains of the two proteins. In order to understand the origins of these distinct exchange rates, we studied the backbone dynamics of both domains in the presence of zinc and of cadmium by NMR spectroscopy. The differential stability of the two metal-binding sites in the RING domains, as reflected by the different metal exchange rates, can be explained by a combination of accessibility and an electrostatic ion interaction model. A greater backbone flexibility for the p44 RING domain as compared to CNOT4 may be related to the distinct types of protein-protein interactions in which the two C4C4 RING domains are involved. © 2005 Elsevier Ltd. All rights reserved.
Databáze: OpenAIRE
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