{"created":"2023-08-02T03:58:05.996815+00:00","id":7244,"links":{},"metadata":{"_buckets":{"deposit":"9be2896e-4279-4165-b793-affaa9a29881"},"_deposit":{"created_by":10,"id":"7244","owners":[10],"pid":{"revision_id":0,"type":"depid","value":"7244"},"status":"published"},"_oai":{"id":"oai:repository.lib.tottori-u.ac.jp:00007244","sets":["1:10","2:12"]},"author_link":["779","1457","2225","26873","26874"],"item_10001_biblio_info_7":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"2019-02-01","bibliographicIssueDateType":"Issued"},"bibliographicIssueNumber":"5","bibliographicPageEnd":"1601","bibliographicPageStart":"1590","bibliographicVolumeNumber":"294","bibliographic_titles":[{"bibliographic_title":"JOURNAL OF BIOLOGICAL CHEMISTRY"},{"bibliographic_title":"JOURNAL OF BIOLOGICAL CHEMISTRY","bibliographic_titleLang":"en"}]}]},"item_10001_description_5":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"The periplasmic small heat shock protein HdeA from Escherichia coli is inactive under normal growth conditions (at pH 7) and activated only when E. coli cells are subjected to a sudden decrease in pH, converting HdeA into an acid-denatured active state. Here, using in vitro fibrillation assays, transmission EM, atomic-force microscopy, and CD analyses, we found that when HdeA is active as a molecular chaperone, it is also capable of forming inactive aggregates that, at first glance, resemble amyloid fibrils. We noted that the molecular chaperone activity of HdeA takes precedence over fibrillogenesis under acidic conditions, as the presence of denatured substrate protein was sufficient to suppress HdeA fibril formation. Further experiments suggested that the secondary structure of HdeA fibrils deviates somewhat from typical amyloid fibrils and contains α-helices. Strikingly, HdeA fibrils that formed at pH 2 were immediately resolubilized by a simple shift to pH 7 and from there could regain molecular chaperone activity upon a return to pH 1. HdeA, therefore, provides an unusual example of a “reversible” form of protein fibrillation with an atypical secondary structure composition. The competition between active assistance of denatured polypeptides (its “molecular chaperone” activity) and the formation of inactive fibrillary deposits (its “fibrillogenic” activity) provides a unique opportunity to probe the relationship among protein function, structure, and aggregation in detail.","subitem_description_type":"Other"}]},"item_10001_publisher_8":{"attribute_name":"出版者","attribute_value_mlt":[{"subitem_publisher":"American Society for Biochemistry and Molecular Biology"}]},"item_10001_relation_14":{"attribute_name":"DOI","attribute_value_mlt":[{"subitem_relation_type":"isIdenticalTo","subitem_relation_type_id":{"subitem_relation_type_id_text":"10.1074/jbc.RA118.005611","subitem_relation_type_select":"DOI"}}]},"item_10001_relation_16":{"attribute_name":"情報源","attribute_value_mlt":[{"subitem_relation_name":[{"subitem_relation_name_text":"Miyawaki Shiori, Uemura Yumi, Hongo Kunihiro, et al. Acid-denatured small heat shock protein HdeA from Escherichia coli forms reversible fibrils with an atypical secondary structure. JOURNAL OF BIOLOGICAL CHEMISTRY. 2019. 294(5). 1590-1601. doi:10.1074/jb"}]}]},"item_10001_relation_17":{"attribute_name":"関連サイト","attribute_value_mlt":[{"subitem_relation_name":[{"subitem_relation_name_text":"https://www.sciencedirect.com/science/article/pii/S0021925820364681"}],"subitem_relation_type_id":{"subitem_relation_type_id_text":"https://www.sciencedirect.com/science/article/pii/S0021925820364681","subitem_relation_type_select":"URI"}}]},"item_10001_rights_15":{"attribute_name":"権利","attribute_value_mlt":[{"subitem_rights":"© 2019 Miyawaki et al. Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc."}]},"item_10001_source_id_9":{"attribute_name":"ISSN","attribute_value_mlt":[{"subitem_source_identifier":"00219258","subitem_source_identifier_type":"ISSN"}]},"item_10001_text_26":{"attribute_name":"EISSN","attribute_value_mlt":[{"subitem_text_value":"1083351X"}]},"item_10001_text_33":{"attribute_name":"著者所属（英）","attribute_value_mlt":[{"subitem_text_language":"en","subitem_text_value":"Graduate School of Sustainability Science, Tottori University"},{"subitem_text_language":"en","subitem_text_value":"Department of Engineering, Tottori University"},{"subitem_text_language":"en","subitem_text_value":"Graduate School of Sustainability Science, Tottori University / Department of Engineering, Tottori University / Center for Research on Green Sustainable Chemistry, Tottori University"},{"subitem_text_language":"en","subitem_text_value":"Graduate School of Sustainability Science, Tottori University / Department of Engineering, Tottori University / Center for Research on Green Sustainable Chemistry, Tottori University"},{"subitem_text_language":"en","subitem_text_value":"Graduate School of Sustainability Science, Tottori University / Department of Engineering, Tottori University / Center for Research on Green Sustainable Chemistry, Tottori University"}]},"item_10001_version_type_20":{"attribute_name":"著者版フラグ","attribute_value_mlt":[{"subitem_version_type":"VoR"}]},"item_creator":{"attribute_name":"著者","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"本郷, 邦広"},{"creatorName":"ホンゴウ, クニヒロ","creatorNameLang":"ja-Kana"},{"creatorName":"Hongo, Kunihiro","creatorNameLang":"en"}],"nameIdentifiers":[{},{},{}]},{"creatorNames":[{"creatorName":"河田, 康志"},{"creatorName":"カワタ, ヤスシ","creatorNameLang":"ja-Kana"},{"creatorName":"Kawata, Yasushi","creatorNameLang":"en"}],"nameIdentifiers":[{},{},{}]},{"creatorNames":[{"creatorName":"溝端, 知宏"},{"creatorName":"ミゾバタ, トモヒロ","creatorNameLang":"ja-Kana"},{"creatorName":"Mizobata, Tomohiro","creatorNameLang":"en"}],"nameIdentifiers":[{},{},{}]},{"creatorNames":[{"creatorName":"Miyawaki, Shiori","creatorNameLang":"en"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Uemura, Yumi","creatorNameLang":"en"}],"nameIdentifiers":[{}]}]},"item_files":{"attribute_name":"ファイル情報","attribute_type":"file","attribute_value_mlt":[{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"2023-03-17"}],"displaytype":"detail","filename":"jbc294(5)_1590.pdf","filesize":[{"value":"4.3 MB"}],"format":"application/pdf","licensefree":"© 2019 Miyawaki et al. Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc.","licensetype":"license_note","mimetype":"application/pdf","url":{"label":"jbc294(5)_1590.pdf","url":"https://repository.lib.tottori-u.ac.jp/record/7244/files/jbc294(5)_1590.pdf"},"version_id":"97ecda7a-36c9-4a7f-9e3e-13a5394e2b51"}]},"item_keyword":{"attribute_name":"キーワード","attribute_value_mlt":[{"subitem_subject":"molecular chaperone","subitem_subject_scheme":"Other"},{"subitem_subject":"protein folding","subitem_subject_scheme":"Other"},{"subitem_subject":"Gram-negative bacteria","subitem_subject_scheme":"Other"},{"subitem_subject":"protein aggregation","subitem_subject_scheme":"Other"},{"subitem_subject":"small heat shock protein (sHsp)","subitem_subject_scheme":"Other"},{"subitem_subject":"amyloid","subitem_subject_scheme":"Other"},{"subitem_subject":"acid denaturation","subitem_subject_scheme":"Other"},{"subitem_subject":"periplasm","subitem_subject_scheme":"Other"},{"subitem_subject":"protein fibrillogenesis","subitem_subject_scheme":"Other"},{"subitem_subject":"reversible fibrillation","subitem_subject_scheme":"Other"},{"subitem_subject":"molecular chaperone","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"protein folding","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"Gram-negative bacteria","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"protein aggregation","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"small heat shock protein (sHsp)","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"amyloid","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"acid denaturation","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"periplasm","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"protein fibrillogenesis","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"reversible fibrillation","subitem_subject_language":"en","subitem_subject_scheme":"Other"}]},"item_language":{"attribute_name":"言語","attribute_value_mlt":[{"subitem_language":"eng"}]},"item_resource_type":{"attribute_name":"資源タイプ","attribute_value_mlt":[{"resourcetype":"journal article"}]},"item_title":"Acid-denatured small heat shock protein HdeA from Escherichia coli forms reversible fibrils with an atypical secondary structure","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"Acid-denatured small heat shock protein HdeA from Escherichia coli forms reversible fibrils with an atypical secondary structure","subitem_title_language":"en"}]},"item_type_id":"10001","owner":"10","path":["12","10"],"pubdate":{"attribute_name":"PubDate","attribute_value":"2022-07-20"},"publish_date":"2022-07-20","publish_status":"0","recid":"7244","relation_version_is_last":true,"title":["Acid-denatured small heat shock protein HdeA from Escherichia coli forms reversible fibrils with an atypical secondary structure"],"weko_creator_id":"10","weko_shared_id":-1},"updated":"2023-09-29T00:41:18.076033+00:00"}