Substitution of the Native Zn(II) with Cd(II), Co(II) and Ni(II) Changes the Downhill Unfolding Mechanism of Ros87 to a Completely Different Scenario.
Agrobacterium tumefaciens
Amino Acid Sequence
Bacterial Proteins
/ chemistry
Binding Sites
/ drug effects
Cadmium
/ chemistry
Cobalt
/ chemistry
DNA-Binding Proteins
/ chemistry
Magnetic Resonance Spectroscopy
Models, Molecular
Nickel
/ chemistry
Protein Folding
/ drug effects
Repressor Proteins
/ chemistry
Spectrophotometry, Ultraviolet
Thermodynamics
Zinc
/ chemistry
Zinc Fingers
cadmium
cobalt
folding mechanism
nickel
zinc finger
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
05 Nov 2020
05 Nov 2020
Historique:
received:
09
10
2020
revised:
30
10
2020
accepted:
03
11
2020
entrez:
10
11
2020
pubmed:
11
11
2020
medline:
9
3
2021
Statut:
epublish
Résumé
The structural effects of zinc replacement by xenobiotic metal ions have been widely studied in several eukaryotic and prokaryotic zinc-finger-containing proteins. The prokaryotic zinc finger, that presents a bigger βββαα domain with a larger hydrophobic core with respect to its eukaryotic counterpart, represents a valuable model protein to study metal ion interaction with metallo-proteins. Several studies have been conducted on Ros87, the DNA binding domain of the prokaryotic zinc finger Ros, and have demonstrated that the domain appears to structurally tolerate Ni(II), albeit with important structural perturbations, but not Pb(II) and Hg(II), and it is in vitro functional when the zinc ion is replaced by Cd(II). We have previously shown that Ros87 unfolding is a two-step process in which a zinc binding intermediate converts to the native structure thorough a delicate downhill folding transition. Here, we explore the folding/unfolding behaviour of Ros87 coordinated to Co(II), Ni(II) or Cd(II), by UV-Vis, CD, DSC and NMR techniques. Interestingly, we show how the substitution of the native metal ion results in complete different folding scenarios. We found a two-state unfolding mechanism for Cd-Ros87 whose metal affinity
Identifiants
pubmed: 33167398
pii: ijms21218285
doi: 10.3390/ijms21218285
pmc: PMC7663847
pii:
doi:
Substances chimiques
Bacterial Proteins
0
DNA-Binding Proteins
0
Repressor Proteins
0
Cadmium
00BH33GNGH
Cobalt
3G0H8C9362
Nickel
7OV03QG267
Zinc
J41CSQ7QDS
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Ministero dell'Istruzione, dell'Università e della Ricerca
ID : 2017WBZFHL
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