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ツゲ ヒデアキ
TSUGE HIDEAKI
津下 英明 所属 京都産業大学 生命科学部 先端生命科学科 職種 教授 |
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| 言語種別 | 英語 |
| 発行・発表の年月 | 2017/10/12 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Involvement of the Arg566 residue of Aeromonas sobria serine protease in substrate specificity |
| 執筆形態 | その他 |
| 掲載誌名 | PLoS One |
| 出版社・発行元 | PUBLIC LIBRARY SCIENCE |
| 巻・号・頁 | 12(10) |
| 著者・共著者 | Hideaki Tsuge |
| 概要 | Aeromonas sobria serine protease (ASP) is an extracellular serine protease secreted by the organism. Here, we identified the amino acid residue of ASP that contributes to substrate specificity by using both synthetic peptides and biological protein components. The results showed that the arginine residue at position 566 (Arg-566) of ASP, which is located in the extra occluding region of ASP close to an entrance of the catalytic cavity, is involved in the substrate specificity. A substitutional point mutation of the Arg-566 residue of ASP to Ala residue (ASP[R566A]) caused a decrease of the proteolytic efficiency for a certain substrate. In addition, ASP lost the ability to recognize the primary substrate by such a point mutation, and ASP[R566A] reacted to a wide range of synthetic substrates. It is likely that Arg-566 causes an interaction with the amino acid residue at position P3 of the substrate, which is the third amino acid residue upstream from the cleavage site. Another study using ORF2 protein, a chaperone protein of ASP, further suggested that Arg-566 could also play an important role in interaction with ORF2. We therefore conclude that the Arg-566 residue of ASP is likely responsible for the selection of substrates. |
| DOI | 10.1371/journal.pone.0186392 |
| ISSN | 1932-6203 |
| PMID | 29023605 |
| Put Code(ORCID) | 40976853 |