{"created":"2023-07-27T06:26:43.196093+00:00","id":10553,"links":{},"metadata":{"_buckets":{"deposit":"76a75f97-5111-47ca-b8a7-d7aae85dea49"},"_deposit":{"created_by":3,"id":"10553","owners":[3],"pid":{"revision_id":0,"type":"depid","value":"10553"},"status":"published"},"_oai":{"id":"oai:kanazawa-u.repo.nii.ac.jp:00010553","sets":["4161:3020:3021"]},"author_link":["16009","16500","15800","2912","16013","13404","2361","16010","16012","98"],"item_4_biblio_info_8":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"2013-10-01","bibliographicIssueDateType":"Issued"},"bibliographicIssueNumber":"1","bibliographicPageEnd":"11","bibliographicPageStart":"2","bibliographicVolumeNumber":"184","bibliographic_titles":[{"bibliographic_title":"Journal of Structural Biology"}]}]},"item_4_creator_33":{"attribute_name":"著者別表示","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"柴田, 幹大"}],"nameIdentifiers":[{},{}]},{"creatorNames":[{"creatorName":"内橋, 貴之"}],"nameIdentifiers":[{},{}]},{"creatorNames":[{"creatorName":"安藤, 敏夫"}],"nameIdentifiers":[{},{}]}]},"item_4_description_21":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"Bacteriorhodopsin (bR) trimers form a two-dimensional hexagonal lattice in the purple membrane of Halobacterium salinarum. However, the physiological significance of forming the lattice has long been elusive. Here, we study this issue by comparing properties of assembled and non-assembled bR trimers using directed mutagenesis, high-speed atomic force microscopy (HS-AFM), optical spectroscopy, and a proton pumping assay. First, we show that the bonds formed between W12 and F135 amino acid residues are responsible for trimer-trimer association that leads to lattice assembly; the lattice is completely disrupted in both W12I and F135I mutants. HS-AFM imaging reveals that both crystallized D96N and non-crystallized D96N/W12I mutants undergo a large conformational change (i.e., outward E-F loop displacement) upon light-activation. However, lattice disruption significantly reduces the rate of conformational change under continuous light illumination. Nevertheless, the quantum yield of M-state formation, measured by low-temperature UV-visible spectroscopy, and proton pumping efficiency are unaffected by lattice disruption. From these results, we conclude that trimer-trimer association plays essential roles in providing bound retinal with an appropriate environment to maintain its full photo-reactivity and in maintaining the natural photo-reaction pathway. © 2013 Elsevier Inc. All rights reserved.","subitem_description_type":"Abstract"}]},"item_4_description_5":{"attribute_name":"提供者所属","attribute_value_mlt":[{"subitem_description":"金沢大学ナノ生命科学研究所","subitem_description_type":"Other"}]},"item_4_identifier_registration":{"attribute_name":"ID登録","attribute_value_mlt":[{"subitem_identifier_reg_text":"10.24517/00010540","subitem_identifier_reg_type":"JaLC"}]},"item_4_publisher_17":{"attribute_name":"出版者","attribute_value_mlt":[{"subitem_publisher":"Elsevier"}]},"item_4_relation_12":{"attribute_name":"DOI","attribute_value_mlt":[{"subitem_relation_type":"isVersionOf","subitem_relation_type_id":{"subitem_relation_type_id_text":"10.1016/j.jsb.2013.02.011","subitem_relation_type_select":"DOI"}}]},"item_4_relation_28":{"attribute_name":"関連URI","attribute_value_mlt":[{"subitem_relation_type_id":{"subitem_relation_type_id_text":"http://www.elsevier.com/locate/issn/10478477","subitem_relation_type_select":"URI"}}]},"item_4_source_id_11":{"attribute_name":"NCID","attribute_value_mlt":[{"subitem_source_identifier":"AA10761632","subitem_source_identifier_type":"NCID"}]},"item_4_source_id_9":{"attribute_name":"ISSN","attribute_value_mlt":[{"subitem_source_identifier":"1047-8477","subitem_source_identifier_type":"ISSN"}]},"item_4_version_type_25":{"attribute_name":"著者版フラグ","attribute_value_mlt":[{"subitem_version_resource":"http://purl.org/coar/version/c_ab4af688f83e57aa","subitem_version_type":"AM"}]},"item_creator":{"attribute_name":"著者","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"Yamashita, Hayato"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Inoue, Keiichi"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Shibata, Mikihiro"}],"nameIdentifiers":[{},{}]},{"creatorNames":[{"creatorName":"Uchihashi, Takayuki"}],"nameIdentifiers":[{},{},{}]},{"creatorNames":[{"creatorName":"Sasaki, Jun"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Kandori, Hideki"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Ando, Toshio"}],"nameIdentifiers":[{},{},{},{}]}]},"item_files":{"attribute_name":"ファイル情報","attribute_type":"file","attribute_value_mlt":[{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"2017-10-03"}],"displaytype":"detail","filename":"SC-PR-ANDO-T-JSB-2.pdf","filesize":[{"value":"1.0 MB"}],"format":"application/pdf","licensetype":"license_11","mimetype":"application/pdf","url":{"label":"SC-PR-ANDO-T-JSB-2.pdf","url":"https://kanazawa-u.repo.nii.ac.jp/record/10553/files/SC-PR-ANDO-T-JSB-2.pdf"},"version_id":"35b51a94-fda3-487d-8bdb-2bd03780ff64"}]},"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","resourceuri":"http://purl.org/coar/resource_type/c_6501"}]},"item_title":"Role of trimer-trimer interaction of bacteriorhodopsin studied by optical spectroscopy and high-speed atomic force microscopy","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"Role of trimer-trimer interaction of bacteriorhodopsin studied by optical spectroscopy and high-speed atomic force microscopy"}]},"item_type_id":"4","owner":"3","path":["3021"],"pubdate":{"attribute_name":"公開日","attribute_value":"2017-10-03"},"publish_date":"2017-10-03","publish_status":"0","recid":"10553","relation_version_is_last":true,"title":["Role of trimer-trimer interaction of bacteriorhodopsin studied by optical spectroscopy and high-speed atomic force microscopy"],"weko_creator_id":"3","weko_shared_id":3},"updated":"2023-07-27T10:16:26.020183+00:00"}