Repository of Research and Investigative Information

Repository of Research and Investigative Information

Ilam University of Medical Sciences

Acid-Induced Formation of Molten Globule States in the Wild Type Escherichia coli 5-Enolpyruvylshikimate 3-Phosphate Synthase and its Three Mutated Forms: G96A, A183T and G96A/A183T

Sat Jun 25 08:37:59 2022

(2011) Acid-Induced Formation of Molten Globule States in the Wild Type Escherichia coli 5-Enolpyruvylshikimate 3-Phosphate Synthase and its Three Mutated Forms: G96A, A183T and G96A/A183T. Protein Journal. pp. 132-137. ISSN 1572-3887

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Abstract

Recent advances in protein chemistry have led to progress in the understanding of protein folding and properties of possible intermediates during the folding of proteins. The molten globule (MG) state, a major intermediate of protein folding, has a denatured state with native-like secondary structure. In the present work, the acid-induced unfolding of wild type Escherichia coli 5-enolpyruvylshikimate 3-phosphate synthase (EPSPS) and its three different variants (G96A, A183T and G96A/A183T) were studied by far- and near-UV circular dichroism (CD), intrinsic fluorescent emission spectroscopy and 1-anilino naphthalene-8-sulfonate (ANS) binding. At pH < 3.0, these EPSPS variants acquire partially folded state, which show the characteristics of the MG state, e.g., a drastic reduction of defined tertiary structure and almost no change in the secondary structure. ANS binding experiments show that hydrophobic surface of these variants is exposed to a greater extent in comparison to the native form, at acidic pH. Wild type, G96A, A183T and G96A/A183T acquire MG states at pH 2.0, 1.5, 3.0 and 3.0, respectively, which show that pH stability of MG state of G96A has increased in comparison to wild type; and pH stability of MG states of two other mutants is lower than that of the wild type. The results suggest that there is a direct relationship between stability of protein and pH stability of its folding intermediates.

Item Type: Article
Creators:
CreatorsEmail
Haghani, K.UNSPECIFIED
Khajeh, K.UNSPECIFIED
Salmanian, A. H.UNSPECIFIED
Ranjbar, B.UNSPECIFIED
Bakhtiyari, S.UNSPECIFIED
Keywords: 5-enolpyruvylshikimate 3-phosphate synthase Molten globule states Stability Circular dichroism 1-anilino naphthalene-8-sulfonate herbicide glyphosate stability enzymes conformation salt Biochemistry & Molecular Biology
Divisions: Education Vice-Chancellor Department > Faculty of Dental
Page Range: pp. 132-137
Journal or Publication Title: Protein Journal
Journal Index: ISI
Volume: 30
Number: 2
Identification Number: https://doi.org/10.1007/s10930-011-9308-2
ISSN: 1572-3887
Depositing User: مهندس مهدی شریفی
URI: http://eprints.medilam.ac.ir/id/eprint/856

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