Molecular mechanism for quality control of bacterial outer membrane by the periplasmic protease BepA

2017 Fiscal Year Final Research Report

• Project/Area Number: 15K07008
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Functional biochemistry
• Research Institution: Morioka College
• Principal Investigator: Narita Shin-ichiro 盛岡大学, 栄養科学部, 教授 (30338751)
• Co-Investigator(Renkei-kenkyūsha): AKIYAMA Yoshinori 京都大学・ウイルス, 再生医科学研究所, 教授 (10192460)
• Research Collaborator: DAIMON Yasushi
• Project Period (FY): 2015-04-01 – 2018-03-31
• Keywords: 細胞内タンパク質分解 / 表層ストレス応答 / 細菌細胞表層 / プロテアーゼ / シャペロン / 外膜タンパク質 / ジスルフィド結合 / タンパク質間相互作用

Outline of Final Research Achievements

BepA is an Escherichia coli periplasmic protease involved in biogenesis and quality control of LptD, a component of the outer membrane lipopolysaccharide translocon. BepA can associate with the BAM complex driving integration of outer membrane proteins into the outer membrane. However, the molecular mechanism of BepA function and its association with the BAM complex remained unknown. In this study, we performed a systematic site-directed in vivo photo-cross-linking analysis to reveal the protein-protein interactions mediated by the BepA TPR domain. We revealed the mode of interaction between the BepA domein and the BAM complex as well as LptD. Mutational analysis indicated that BepA TPR domain is essential and protein-protein interactions mediated by the TPR domain is critical for the function of BepA.

Free Research Field

機能生物化学