Please use this identifier to cite or link to this item:
|Title:||Unexpected functional implication of a stable succinimide in the structural stability of Methanocaldococcus jannaschii glutaminase|
|Publisher:||Nature Publishing Group|
|Citation:||Kumar, S.; Prakash, S.; Gupta, K.; Dongre, A.; Balaram, P.; Balaram, H., Unexpected functional implication of a stable succinimide in the structural stability of Methanocaldococcus jannaschii glutaminase. Nature Communications 2016, 7, 14 http://dx.doi.org/10.1038/ncomms12798|
|Abstract:||Protein ageing is often mediated by the formation of succinimide intermediates. These short-lived intermediates derive from asparaginyl deamidation and aspartyl dehydration and are rapidly converted into beta-aspartyl or D-aspartyl residues. Here we report the presence of a highly stable succinimide intermediate in the glutaminase subunit of GMP synthetase from the hyperthermophile Methanocaldoccocus jannaschii. By comparing the biophysical properties of the wild-type protein and of several mutants, we show that the presence of succinimide increases the structural stability of the glutaminase subunit. The protein bearing this modification in fact remains folded at 100 degrees C and in 8M guanidinium chloride. Mutation of the residue following the reactive asparagine provides insight into the factors that contribute to the hydrolytic stability of the succinimide. Our findings suggest that sequences that stabilize succinimides from hydrolysis may be evolutionarily selected to confer extreme thermal stability.|
|Appears in Collections:||Research Papers (Hemalatha Balaram)|
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.