{"created":"2023-05-15T16:43:04.325948+00:00","id":18273,"links":{},"metadata":{"_buckets":{"deposit":"43c47caa-bdf6-4405-a7c4-19f81133f659"},"_deposit":{"created_by":2,"id":"18273","owners":[2],"pid":{"revision_id":0,"type":"depid","value":"18273"},"status":"published"},"_oai":{"id":"oai:nagasaki-u.repo.nii.ac.jp:00018273","sets":["27:28"]},"author_link":["72954","72952","72953","72955"],"item_2_biblio_info_6":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"2003-01","bibliographicIssueDateType":"Issued"},"bibliographicIssueNumber":"1","bibliographicPageEnd":"154","bibliographicPageStart":"146","bibliographicVolumeNumber":"270","bibliographic_titles":[{"bibliographic_title":"European journal of biochemistry / FEBS"}]}]},"item_2_description_4":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"The alpha isoform of human 90-kDa heat shock protein (HSP90alpha) is composed of three domains: the N-terminal (residues 1-400); middle (residues 401-615) and C-terminal (residues 621-732). The middle domain is simultaneously associated with the N- and C-terminal domains, and the interaction with the latter mediates the dimeric configuration of HSP90. Besides one in the N-terminal domain, an additional client-binding site exists in the C-terminal domain of HSP90. The aim of the present study is to elucidate the regions within the C-terminal domain responsible for the bindings to the middle domain and to a client protein, and to define the relationship between the two functions. A bacterial two-hybrid system revealed that residues 650-697 of HSP90alpha were essential for the binding to the middle domain. An almost identical region (residues 657-720) was required for the suppression of heat-induced aggregation of citrate synthase, a model client protein. Replacement of either Leu665-Leu666 or Leu671-Leu672 to Ser-Ser within the hydrophobic segment (residues 662-678) of the C-terminal domain caused the loss of bindings to both the middle domain and the client protein. The interaction between the middle and C-terminal domains was also found in human 94-kDa glucose-regulated protein. Moreover, Escherichia coli HtpG, a bacterial HSP90 homologue, formed heterodimeric complexes with HSP90alpha and the 94-kDa glucose-regulated protein through their middle-C-terminal domains. Taken together, it is concluded that the identical region including the hydrophobic segment of the C-terminal domain is essential for both the client binding and dimer formation of the HSP90-family molecular chaperone and that the dimeric configuration appears to be similar in the HSP90-family proteins.","subitem_description_type":"Abstract"}]},"item_2_description_63":{"attribute_name":"引用","attribute_value_mlt":[{"subitem_description":"European journal of biochemistry, 270(1), pp.146-154; 2003","subitem_description_type":"Other"}]},"item_2_publisher_33":{"attribute_name":"出版者","attribute_value_mlt":[{"subitem_publisher":"Blackwell Science"}]},"item_2_relation_11":{"attribute_name":"PubMed番号","attribute_value_mlt":[{"subitem_relation_type":"isVersionOf","subitem_relation_type_id":{"subitem_relation_type_id_text":"12492485","subitem_relation_type_select":"PMID"}}]},"item_2_relation_12":{"attribute_name":"DOI","attribute_value_mlt":[{"subitem_relation_type":"isVersionOf","subitem_relation_type_id":{"subitem_relation_type_id_text":"10.1046/j.1432-1033.2003.03375.x","subitem_relation_type_select":"DOI"}}]},"item_2_source_id_10":{"attribute_name":"書誌レコードID","attribute_value_mlt":[{"subitem_source_identifier":"AA00639541","subitem_source_identifier_type":"NCID"}]},"item_2_source_id_7":{"attribute_name":"ISSN","attribute_value_mlt":[{"subitem_source_identifier":"00142956","subitem_source_identifier_type":"ISSN"}]},"item_2_version_type_16":{"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":"Yamada, Shin-ichi"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Ono, Toshio"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Mizuno, Akio"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Nemoto, Takayuki K"}],"nameIdentifiers":[{}]}]},"item_files":{"attribute_name":"ファイル情報","attribute_type":"file","attribute_value_mlt":[{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"2020-12-23"}],"displaytype":"detail","filename":"EJB27_1_146.pdf","filesize":[{"value":"412.5 kB"}],"format":"application/pdf","licensetype":"license_note","mimetype":"application/pdf","url":{"label":"EJB27_1_146.pdf","url":"https://nagasaki-u.repo.nii.ac.jp/record/18273/files/EJB27_1_146.pdf"},"version_id":"585c501c-369f-48bc-8da5-6289d0fc0697"}]},"item_keyword":{"attribute_name":"キーワード","attribute_value_mlt":[{"subitem_subject":"GRP94","subitem_subject_scheme":"Other"},{"subitem_subject":"HtpG","subitem_subject_scheme":"Other"},{"subitem_subject":"molecular chaperone","subitem_subject_scheme":"Other"},{"subitem_subject":"dimer","subitem_subject_scheme":"Other"},{"subitem_subject":"client binding","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","resourceuri":"http://purl.org/coar/resource_type/c_6501"}]},"item_title":"A hydrophobic segment within the C-terminal domain is essential for both client-binding and dimer formation of the HSP90-family molecular chaperone.","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"A hydrophobic segment within the C-terminal domain is essential for both client-binding and dimer formation of the HSP90-family molecular chaperone."}]},"item_type_id":"2","owner":"2","path":["28"],"pubdate":{"attribute_name":"公開日","attribute_value":"2008-10-16"},"publish_date":"2008-10-16","publish_status":"0","recid":"18273","relation_version_is_last":true,"title":["A hydrophobic segment within the C-terminal domain is essential for both client-binding and dimer formation of the HSP90-family molecular chaperone."],"weko_creator_id":"2","weko_shared_id":-1},"updated":"2023-05-16T04:02:42.767572+00:00"}