High affinity of recombinant DJ-1 (PARK7) protein to Ni-NTA
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Authors
A. Mussakhmetov
National Center for Biotechnology,13/5, Korgalzhyn road, Nur-Sultan, 010000, Kazakhstan
L.N. Gumilyov Eurasian National University, 2 Satpayev str., Nur-Sultan, 010008, Kazakhstan
D. Utepbergenov
Nazarbayev University, Kabanbay batyr ave 53, Nur-Sultan, 010000, Kazakhstan
B. Khassenov, National center for biotechnology
National Center for Biotechnology,13/5, Korgalzhyn road, Nur-Sultan, 010000, Kazakhstan
Abstract
The DJ-1 protein also known as Parkinson disease protein 7 (PARK7) is a glyoxalase associated with hereditary form of Parkinson's disease. Glyoxalase DJ-1 consists of 189 amino acids and has a molecular weight of 20 kDa. The physiological role of DJ-1 is unclear but recent evidence suggest that it can detoxify reactive electrophiles formed in glycolysis. Expression and purification of the recombinant DJ-1 protein in Escherichia coli revealed an abnormally high affinity of rDJ-1 for Ni-NTA, which was accompanied by a color change of Ni-NTA from blue to blue-violet. rDJ-1 formed the strong complex with Ni-NTA, which was destroyed only by 2400 mM imidazole. Experiments with the mutant DJ-1 protein containing the Cys106Ser substitution confirmed the key role of cysteine at position 106 for the formation of this complex. The discovered phenomenon shows the potential of using the DJ-1-tag as a protein tag for obtaining high-purity protein preparations and for bioanalytical applications.
Keywords
Parkinson disease, recombinant protein, affinity chromatography, DJ-1 protein
Article Details
References
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