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Generation of a Functionally Distinct Rhizopus oryzae Lipase through Protein Folding Memory.
- Source :
- PLoS ONE; May2015, Vol. 10 Issue 5, p1-13, 13p
- Publication Year :
- 2015
-
Abstract
- Rhizopus oryzae lipase (ROL) has a propeptide at its N-terminus that functions as an intramolecular chaperone and facilitates the folding of mature ROL (mROL). In this study, we successfully generated a functionally distinct imprinted mROL (mROL<superscript>imp</superscript>) through protein folding memory using a mutated propeptide. The mutated propeptide left its structural memory on mROL and produced mROL<superscript>imp</superscript> that exhibited different substrate specificities compared with mROL<superscript>WT</superscript> (prepared from the wild type propeptide), although the amino acid sequences of both mROLs were the same. mROL<superscript>imp</superscript> showed a preference for substrates with medium chain-length acyl groups and, noticeably, recognized a peptidase-specific substrate. In addition, ROL<superscript>imp</superscript> was more stable than mROL<superscript>WT</superscript>. These results strongly suggest that proteins with identical amino acid sequences can fold into different conformations and that mutations in intramolecular chaperones can dynamically induce changes in enzymatic activity. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 19326203
- Volume :
- 10
- Issue :
- 5
- Database :
- Complementary Index
- Journal :
- PLoS ONE
- Publication Type :
- Academic Journal
- Accession number :
- 102970335
- Full Text :
- https://doi.org/10.1371/journal.pone.0124545