期刊
EXTREMOPHILES
卷 19, 期 3, 页码 681-691出版社
SPRINGER JAPAN KK
DOI: 10.1007/s00792-015-0748-z
关键词
Sequential folding; Subunit interaction; Co-operativity; Stability; Domain; Multimeric
资金
- CSIR-INDIA
- ICMR Govt. of INDIA
- IIT Delhi
Here, we report the folding and assembly of a Pyrococcus furiosus-derived protein, l-asparaginase (PfA). PfA functions as a homodimer, with each monomer made of distinct N- and C-terminal domains. The purified individual domains as well as single Trp mutant of each domain were subjected to chemical denaturation/renaturation and probed by combination of spectroscopic, chromatographic, quenching and scattering techniques. We found that the N-domain acts like a folding scaffold and assists the folding of remaining polypeptide. The domains displayed sequential folding with the N-domain having higher thermodynamic stability. We report that the extreme thermal stability of PfA is due to the presence of high intersubunit associative forces supported by extensive H-bonding and ionic interactions network. Our results proved that folding cooperativity in a thermophilic, multisubunit protein is dictated by concomitant folding and association of constituent domains directly into a native quaternary structure. This report gives an account of the factors responsible for folding and stability of a therapeutically and industrially important protein.
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