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The TPR domain of BepA is required for productive interaction with substrate proteins and the β-barrel assembly machinery complex

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dc.contributor.author Daimon, Yasushi
dc.contributor.author Iwama-Masui, Chigusa
dc.contributor.author Tanaka, Yoshiki
dc.contributor.author Shiota, Takuya
dc.contributor.author Suzuki, Takehiro
dc.contributor.author Miyazaki, Ryoji
dc.contributor.author Sakurada, Hiroto
dc.contributor.author Lithgow, Trevor
dc.contributor.author Dohmae, Naoshi
dc.contributor.author Mori, Hiroyuki
dc.contributor.author Tsukazaki, Tomoya
dc.contributor.author Narita, Shin-ichiro
dc.contributor.author Akiyama, Yoshinori
dc.date.accessioned 2018-03-07T05:32:05Z
dc.date.available 2018-03-07T05:32:05Z
dc.date.issued 2017-10-17
dc.identifier.issn 1365-2958
dc.identifier.uri http://hdl.handle.net/10061/12211
dc.description.abstract BepA (formerly YfgC) is an Escherichia coli periplasmic protein consisting of an N-terminal protease domain and a C-terminal tetratricopeptide repeat (TPR) domain. We have previously shown that BepA is a dual functional protein with chaperone-like and proteolytic activities involved in membrane assembly and proteolytic quality control of LptD, a major component of the outer membrane lipopolysaccharide translocon. Intriguingly, BepA can associate with the BAM complex: the β-barrel assembly machinery (BAM) driving integration of β-barrel proteins into the outer membrane. However, the molecular mechanism of BepA function and its association with the BAM complex remains unclear. Here, we determined the crystal structure of the BepA TPR domain, which revealed the presence of two subdomains formed by four TPR motifs. Systematic site-directed in vivo photo-cross-linking was used to map the protein–protein interactions mediated by the BepA TPR domain, showing that this domain interacts both with a substrate and with the BAM complex. Mutational analysis indicated that these interactions are important for the BepA functions. These results suggest that the TPR domain plays critical roles in BepA functions through interactions both with substrates and with the BAM complex. Our findings provide insights into the mechanism of biogenesis and quality control of the outer membrane. ja_JP
dc.language.iso en ja_JP
dc.publisher John Wiley & Sons, Ltd ja_JP
dc.rights © 2017 John Wiley & Sons Ltd ja_JP
dc.rights 出版者許諾条件により、本文は2018年10月17日以降公開。 ja_JP
dc.rights This is the peer reviewed version of the following article: http://onlinelibrary.wiley.com/doi/10.1111/mmi.13844/full, which has been published in final form at http://dx.doi.org/ 10.1111/mmi.13844 . This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving. ja_JP
dc.title The TPR domain of BepA is required for productive interaction with substrate proteins and the β-barrel assembly machinery complex ja_JP
dc.type.nii Journal Article ja_JP
dc.contributor.transcription タナカ, ヨシキ
dc.contributor.transcription サクラダ, ヒロト
dc.contributor.transcription ツカザキ, トモヤ
dc.contributor.alternative 田中, 良樹
dc.contributor.alternative 櫻田, 洋人
dc.contributor.alternative 塚崎, 智也
dc.identifier.fulltexturl http://onlinelibrary.wiley.com/doi/10.1111/mmi.13844/full ja_JP
dc.textversion author ja_JP
dc.identifier.jtitle Molecular Microbiology ja_JP
dc.identifier.volume 106 ja_JP
dc.identifier.issue 5 ja_JP
dc.identifier.spage 760 ja_JP
dc.identifier.epage 776 ja_JP
dc.relation.doi info:doi/10.1111/mmi.13844 ja_JP
dc.identifier.NAIST-ID 74650169 ja_JP
dc.identifier.NAIST-ID 84365667 ja_JP
dc.identifier.NAIST-ID 73299737 ja_JP
dc.relation.pmid 28960545 ja_JP

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