Dimerization ability, denaturation mechanism, and the stability of a staphylococcal phage repressor and its two domains

Autor: Anindya Biswas, Semanti Ghosh, Anindya Dutta, Soham Seal, Debabrata Sinha, Angshuman Bagchi, Subrata Sau
Rok vydání: 2019
Předmět:
Models
Molecular
Protein Conformation
alpha-Helical
Protein Folding
Staphylococcus aureus
Stereochemistry
Dimer
Genetic Vectors
Equilibrium unfolding
Gene Expression
Repressor
02 engineering and technology
Molecular Dynamics Simulation
Biochemistry
Substrate Specificity
law.invention
Viral Proteins
03 medical and health sciences
chemistry.chemical_compound
Bacterial Proteins
Structural Biology
law
Lysogenic cycle
Escherichia coli
Protein Interaction Domains and Motifs
Denaturation (biochemistry)
Cloning
Molecular
Lysogeny
Molecular Biology
030304 developmental biology
0303 health sciences
Binding Sites
Aqueous solution
General Medicine
021001 nanoscience & nanotechnology
Recombinant Proteins
Repressor Proteins
Folding (chemistry)
Kinetics
chemistry
Recombinant DNA
Thermodynamics
Protein Conformation
beta-Strand
Protein Multimerization
Staphylococcus Phages
0210 nano-technology
Hydrophobic and Hydrophilic Interactions
Protein Binding
Zdroj: International Journal of Biological Macromolecules. 124:903-914
ISSN: 0141-8130
DOI: 10.1016/j.ijbiomac.2018.11.263
Popis: The lysogenic growth of phage ф11 in Staphylococcus aureus is controlled by a repressor (CI) that harbors an N-terminal domain (NTD), and a C-terminal domain (CTD). Previously, NTD, like CI, showed DNA binding activity and dimerized in the aqueous solution. To precisely understand the folding mechanism, function, and the stability of CI, NTD, and CTD, we have investigated their recombinant forms, rCI, rNTD, and rCTD, using various probes. The data reveal that rCTD, like rCI and rNTD, is a well-structured protein and produces dimers in the aqueous environment. However, the stability order of the dimers appears to be rCI > rCTD > rNTD. Interestingly, the stability of rNTD or rCTD looks slightly higher than that of rCI. The urea-induced equilibrium unfolding of these proteins proceeded via the production of two intermediates. The structure, surface hydrophobicity, and the dimeric status of one intermediate mostly differed from those of another intermediate or the native protein. Our MD simulation study on the representative NTD shows the substantial change in its structure and stability at the urea concentrations, which formed rNTD intermediates. Collectively, the computational data have supported the experimental data and indicated that the CI and its domains are folded by a similar multiphasic pathway.
Databáze: OpenAIRE
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