NDLI: S95C substitution in CuZn-SOD of Ipomoea carnea: impact on the structure, function and stability

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Mishra, Panchanand Satpati, Suresh Baral, Sudhira Kumar Dixit, Anshuman Sabat, Surendra Chandra
Description	Country affiliation: India Author Affiliation: Mishra P ( Department of Gene Function and Regulation, Stress Biology Laboratory, Institute of Life Sciences, Nalco Square, Chandrasekharpur, Bhubaneswar-751023, Odisha, India. surendrachandra@gmail.com.)
Abstract	Superoxide dismutase (SOD) in general is a unique homo-dimeric enzyme that can scavenge toxic superoxide radicals by dismutation reaction. In IcSOD (Ipomoea carnea SOD), the presence of cysteine (Cys) plays an essential role in protein behaviour. This study analysed the role of Cys in modulating the stability and kinetic properties of IcSOD. To investigate the significance of the dimeric structure in modulating the structure/function relationship of CuZn-SODs, we have substituted a conserved serine by cysteine (Ser95Cys) in Ipomoea carnea CuZn-SOD. The results demonstrate that this mutation leads to an increase in dimeric strength, as reflected by size exclusion chromatography, differential scanning calorimetry, and high-temperature circular dichroism spectroscopy measurements. The mutant form, as compared to the native enzyme, shows a relatively low tendency to form aggregates but encountered a reduction in both dismutase and peroxidase activities. This study provides new mechanistic insight into the role of free cysteine in CuZn-SODs and such mutation may be used to increase dimeric strength. Protein docking and molecular dynamics simulations further demonstrate that Ser95Cys substitution in Ipomoea carnea CuZn-SOD leads to the creation of a new subunit interface resulting in increased dimeric strength of the protein.
File Format	HTM / HTML
ISSN	1742206X
Issue Number	10
Journal	Molecular BioSystems
Volume Number	12
e-ISSN	17422051
Language	English
Publisher	Royal Society of Chemistry
Publisher Date	2016-10-20
Publisher Place	Great Britain (UK)
Access Restriction	Subscribed
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Biotechnology

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