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Publication Abstract from PubMed

Nylon hydrolase (NylC) is initially expressed as an inactive precursor (36 kDa). The precursor is cleaved autocatalytically at Asn266/Thr267 to generate an active enzyme composed of an alpha subunit (27 kDa) and a beta subunit (9 kDa). Four alphabeta heterodimers (molecules A-D) form a doughnut-shaped quaternary structure. In this study, the thermostability of the parental NylC was altered by amino acid substitutions located at the A/D interface (D122G/H130Y/D36A/L137A) or the A/B interface (E263Q) and spanned a range of 47 degrees C. Considering structural, biophysical, and biochemical analyses, we discuss the structural basis of the stability of nylon hydrolase. From the analytical centrifugation data obtained regarding the various mutant enzymes, we conclude that the assembly of the monomeric units is dynamically altered by the mutations. Finally, we propose a model that can predict whether the fate of the nascent polypeptide will be correct subunit assembly, inappropriate protein-protein interactions causing aggregation, or intracellular degradation of the polypeptide.

Structural basis of the correct subunit assembly, aggregation, and intracellular degradation of nylon hydrolase.,Negoro S, Shibata N, Lee YH, Takehara I, Kinugasa R, Nagai K, Tanaka Y, Kato DI, Takeo M, Goto Y, Higuchi Y Sci Rep. 2018 Jun 27;8(1):9725. doi: 10.1038/s41598-018-27860-w. PMID:29950566^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.