Effects of ionic strength on the folding and stability of SAMP1, a ubiquitin-like halophilic protein.
Journal
Biophysical journal
ISSN: 1542-0086
Titre abrégé: Biophys J
Pays: United States
ID NLM: 0370626
Informations de publication
Date de publication:
15 02 2022
15 02 2022
Historique:
received:
27
07
2021
revised:
13
12
2021
accepted:
13
01
2022
pubmed:
23
1
2022
medline:
15
4
2022
entrez:
22
1
2022
Statut:
ppublish
Résumé
Our knowledge of the folding behavior of proteins from extremophiles is limited at this time. These proteins may more closely resemble the primordial proteins selected in early evolution under extreme conditions. The small archaeal modifier protein 1 (SAMP1) studied in this report is an 87-residue protein with a β-grasp fold found in the halophile Haloferax volcanii from the Dead Sea. To gain insight into the effects of salt on the stability and folding mechanism of SAMP1, we conducted equilibrium and kinetic folding experiments as a function of sodium chloride concentration. The results revealed that increasing ionic strength accelerates refolding and slows down unfolding of SAMP1, giving rise to a pronounced salt-induced stabilization. With increasing NaCl concentration, the rate of folding observed via a combination of continuous-flow (0.1-2 ms time range) and stopped-flow measurements (>2 ms) exhibited a >100-fold increase between 0.1 and 1.5 M NaCl and leveled off at higher concentrations. Using the Linderström-Lang smeared charge formalism to model electrostatic interactions in ground and transition states encountered during folding, we showed that the observed salt dependence is dominated by Debye-Hückel screening of electrostatic repulsion among numerous negatively charged residues. Comparisons are also drawn with three well-studied mesophilic members of the β-grasp superfamily: protein G, protein L, and ubiquitin. Interestingly, the folding rate of SAMP1 in 3 M sodium chloride is comparable to that of protein G, ubiquitin, and protein L at lower ionic strength. The results indicate the important role of electrostatic interactions in protein folding and imply that proteins have evolved to minimize unfavorable charge-charge interactions under their specific native conditions.
Identifiants
pubmed: 35063455
pii: S0006-3495(22)00039-X
doi: 10.1016/j.bpj.2022.01.010
pmc: PMC8874027
pii:
doi:
Substances chimiques
Membrane Proteins
0
Nuclear Proteins
0
Ubiquitin
0
Ubiquitins
0
Sodium Chloride
451W47IQ8X
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
552-564Subventions
Organisme : NCI NIH HHS
ID : P30 CA006927
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM116911
Pays : United States
Informations de copyright
Copyright © 2022 Biophysical Society. Published by Elsevier Inc. All rights reserved.
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