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Title: Generation of a functionally distinct Rhizopus oryzae lipase through protein folding memory
Authors: Satomura, Atsushi
Kuroda, Kouichi
Ueda, Mitsuyoshi
Author's alias: 里村, 淳
黒田, 浩一
植田, 充美
Issue Date: 13-May-2015
Publisher: Public Library of Science
Journal title: PLOS ONE
Volume: 10
Issue: 5
Thesis number: e0124545
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[imp]) through protein folding memory using a mutated propeptide. The mutated propeptide left its structural memory on mROL and produced mROL[imp] that exhibited different substrate specificities compared with mROL[WT] (prepared from the wild type propeptide), although the amino acid sequences of both mROLs were the same. mROL[imp] showed a preference for substrates with medium chain-length acyl groups and, noticeably, recognized a peptidase-specific substrate. In addition, ROL[imp] was more stable than mROL[WT]. 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.
Description: アンフィンセン説を覆す酵素タンパク質リパーゼの創製に成功. 京都大学プレスリリース. 2015-05-18.
Rights: © 2015 Satomura et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited
URL: http://www.kyoto-u.ac.jp/ja/research/research_results/2015/150514_2.html
URI: http://hdl.handle.net/2433/210282
DOI(Published Version): 10.1371/journal.pone.0124545
PubMed ID: 25970342
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