ログイン
言語:

WEKO3

  • トップ
  • ランキング
To
lat lon distance
To

Field does not validate



インデックスリンク

インデックスツリー

メールアドレスを入力してください。

WEKO

One fine body…

WEKO

One fine body…

アイテム

{"_buckets": {"deposit": "cd9f7958-082b-43d8-ac8e-e5702a85576c"}, "_deposit": {"created_by": 21, "id": "4302", "owners": [21], "pid": {"revision_id": 0, "type": "depid", "value": "4302"}, "status": "published"}, "_oai": {"id": "oai:ir.soken.ac.jp:00004302", "sets": ["323"]}, "author_link": ["2364", "2361", "2512", "2495"], "item_10001_biblio_info_7": {"attribute_name": "書誌情報", "attribute_value_mlt": [{"bibliographicIssueDates": {"bibliographicIssueDate": "2001-09-21", "bibliographicIssueDateType": "Issued"}, "bibliographicIssueNumber": "3", "bibliographicPageEnd": "567", "bibliographicPageStart": "555", "bibliographicVolumeNumber": "312", "bibliographic_titles": [{"bibliographic_title": "Journal of Molecular Biology"}, {"bibliographic_title": "Journal of Molecular Biology", "bibliographic_titleLang": "en"}]}]}, "item_10001_creator_3": {"attribute_name": "著者別名", "attribute_type": "creator", "attribute_value_mlt": [{"creatorNames": [{"creatorName": "桑島, 邦博"}], "nameIdentifiers": [{"nameIdentifier": "2364", "nameIdentifierScheme": "WEKO"}, {"nameIdentifier": "1000070091444", "nameIdentifierScheme": "NRID", "nameIdentifierURI": " "}, {"nameIdentifier": "70091444", "nameIdentifierScheme": "e-Rad", "nameIdentifierURI": "https://kaken.nii.ac.jp/ja/search/?qm=70091444"}]}]}, "item_10001_description_5": {"attribute_name": "抄録", "attribute_value_mlt": [{"subitem_description": "We studied the refolding kinetics of α-lactalbumin in the presence of wild-type GroEL and its ATPase-deficient mutant D398A at various concentrations of nucleotides (ATP and ADP). We evaluated the apparent binding constant between GroEL and the α-lactalbumin refolding intermediate quantitatively by numerical simulation analysis of the α-lactalbumin refolding curves in the presence and absence of GroEL. The binding constant showed a co-operative decrease with an increase in ATP concentration, whereas the binding constant decreased in a non-co-operative manner with respect to ADP concentration. For the D398A mutant, the ATP-induced decrease in affinity occurred much faster than the steady-state ATP hydrolysis by this mutant, suggesting that ATP binding to GroEL rather than ATP hydrolysis, was responsible for the co-operative decrease in the affinity for the target protein. We thus analyzed the nucleotide-concentration dependence of affinity of GroEL for the target protein using an allosteric Monod-Wyman-Changeux model in which GroEL underwent an ATP-induced co-operative conformational transition between the high-affinity and low-affinity states of the target protein. The transition midpoint of the ATP-induced transition of GroEL has been found to be around 30 μM, in good agreement with the midpoint evaluated in other structural studies of GroEL. The results show that the observed difference between ATP and ADP-induced transitions of GroEL are brought about by a small difference in an allosteric parameter (the ratio of the nucleotide affinities of GroEL in the high-affinity and the low-affinity states), i.e. 4.1 for ATP and 2.6 for ADP.", "subitem_description_type": "Abstract"}]}, "item_10001_publisher_8": {"attribute_name": "出版者", "attribute_value_mlt": [{"subitem_publisher": "Elsevier "}]}, "item_10001_relation_14": {"attribute_name": "DOI", "attribute_value_mlt": [{"subitem_relation_name": [{"subitem_relation_name_text": "10.1006/jmbi.2001.4959"}], "subitem_relation_type_id": {"subitem_relation_type_id_text": "https://doi.org/10.1006/jmbi.2001.4959", "subitem_relation_type_select": "DOI"}}]}, "item_10001_rights_15": {"attribute_name": "権利", "attribute_value_mlt": [{"subitem_rights": "© 2001 Academic Press"}]}, "item_10001_source_id_9": {"attribute_name": "ISSN", "attribute_value_mlt": [{"subitem_source_identifier": "0022-2836 ", "subitem_source_identifier_type": "ISSN"}]}, "item_access_right": {"attribute_name": "アクセス権", "attribute_value_mlt": [{"subitem_access_right": "metadata only access", "subitem_access_right_uri": "http://purl.org/coar/access_right/c_14cb"}]}, "item_creator": {"attribute_name": "著者", "attribute_type": "creator", "attribute_value_mlt": [{"creatorNames": [{"creatorName": "TADASHI, Makio"}], "nameIdentifiers": [{"nameIdentifier": "2495", "nameIdentifierScheme": "WEKO"}]}, {"creatorNames": [{"creatorName": "TAKASU-ISHIKAWA, Etsuko "}], "nameIdentifiers": [{"nameIdentifier": "2512", "nameIdentifierScheme": "WEKO"}]}, {"creatorNames": [{"creatorName": "KUWAJIMA, Kunihiro "}], "nameIdentifiers": [{"nameIdentifier": "2361", "nameIdentifierScheme": "WEKO"}]}]}, "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": "Nucleotide-induced Transition of GroEL from the High-affinity to the Low-affinity State for a Target Protein: Effects of ATP and ADP on the GroEL-affected Refolding of α-Lactalbumin", "item_titles": {"attribute_name": "タイトル", "attribute_value_mlt": [{"subitem_title": "Nucleotide-induced Transition of GroEL from the High-affinity to the Low-affinity State for a Target Protein: Effects of ATP and ADP on the GroEL-affected Refolding of α-Lactalbumin"}, {"subitem_title": "Nucleotide-induced Transition of GroEL from the High-affinity to the Low-affinity State for a Target Protein: Effects of ATP and ADP on the GroEL-affected Refolding of α-Lactalbumin", "subitem_title_language": "en"}]}, "item_type_id": "10001", "owner": "21", "path": ["323"], "permalink_uri": "https://ir.soken.ac.jp/records/4302", "pubdate": {"attribute_name": "公開日", "attribute_value": "2014-03-17"}, "publish_date": "2014-03-17", "publish_status": "0", "recid": "4302", "relation": {}, "relation_version_is_last": true, "title": ["Nucleotide-induced Transition of GroEL from the High-affinity to the Low-affinity State for a Target Protein: Effects of ATP and ADP on the GroEL-affected Refolding of α-Lactalbumin"], "weko_shared_id": 21}
  1. 010 学術雑誌論文
  2. 桑島, 邦博 / KUWAJIMA, Kunihiro

Nucleotide-induced Transition of GroEL from the High-affinity to the Low-affinity State for a Target Protein: Effects of ATP and ADP on the GroEL-affected Refolding of α-Lactalbumin

https://ir.soken.ac.jp/records/4302
https://ir.soken.ac.jp/records/4302
045ff364-3bdc-4766-8bb4-dfff1f7e20f6
Item type 学術雑誌論文 / Journal Article(1)
公開日 2014-03-17
タイトル
タイトル Nucleotide-induced Transition of GroEL from the High-affinity to the Low-affinity State for a Target Protein: Effects of ATP and ADP on the GroEL-affected Refolding of α-Lactalbumin
タイトル
言語 en
タイトル Nucleotide-induced Transition of GroEL from the High-affinity to the Low-affinity State for a Target Protein: Effects of ATP and ADP on the GroEL-affected Refolding of α-Lactalbumin
言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ journal article
アクセス権
アクセス権 metadata only access
アクセス権URI http://purl.org/coar/access_right/c_14cb
著者 TADASHI, Makio

× TADASHI, Makio

WEKO 2495

TADASHI, Makio

Search repository
TAKASU-ISHIKAWA, Etsuko

× TAKASU-ISHIKAWA, Etsuko

WEKO 2512

TAKASU-ISHIKAWA, Etsuko

Search repository
KUWAJIMA, Kunihiro

× KUWAJIMA, Kunihiro

WEKO 2361

KUWAJIMA, Kunihiro

Search repository
著者別名 桑島, 邦博

× 桑島, 邦博

WEKO 2364
NRID 1000070091444
e-Rad 70091444

桑島, 邦博

Search repository
抄録
内容記述タイプ Abstract
内容記述 We studied the refolding kinetics of α-lactalbumin in the presence of wild-type GroEL and its ATPase-deficient mutant D398A at various concentrations of nucleotides (ATP and ADP). We evaluated the apparent binding constant between GroEL and the α-lactalbumin refolding intermediate quantitatively by numerical simulation analysis of the α-lactalbumin refolding curves in the presence and absence of GroEL. The binding constant showed a co-operative decrease with an increase in ATP concentration, whereas the binding constant decreased in a non-co-operative manner with respect to ADP concentration. For the D398A mutant, the ATP-induced decrease in affinity occurred much faster than the steady-state ATP hydrolysis by this mutant, suggesting that ATP binding to GroEL rather than ATP hydrolysis, was responsible for the co-operative decrease in the affinity for the target protein. We thus analyzed the nucleotide-concentration dependence of affinity of GroEL for the target protein using an allosteric Monod-Wyman-Changeux model in which GroEL underwent an ATP-induced co-operative conformational transition between the high-affinity and low-affinity states of the target protein. The transition midpoint of the ATP-induced transition of GroEL has been found to be around 30 μM, in good agreement with the midpoint evaluated in other structural studies of GroEL. The results show that the observed difference between ATP and ADP-induced transitions of GroEL are brought about by a small difference in an allosteric parameter (the ratio of the nucleotide affinities of GroEL in the high-affinity and the low-affinity states), i.e. 4.1 for ATP and 2.6 for ADP.
書誌情報 Journal of Molecular Biology
en : Journal of Molecular Biology

巻 312, 号 3, p. 555-567, 発行日 2001-09-21
出版者
出版者 Elsevier
ISSN
収録物識別子タイプ ISSN
収録物識別子 0022-2836
DOI
識別子タイプ DOI
関連識別子 https://doi.org/10.1006/jmbi.2001.4959
関連名称 10.1006/jmbi.2001.4959
権利
権利情報 © 2001 Academic Press
戻る
0
views
See details
Views

Versions

Ver.1 2023-06-20 14:25:27.863359
Show All versions

Share

Mendeley Twitter Facebook Print Addthis

Cite as

エクスポート

OAI-PMH
  • OAI-PMH JPCOAR
  • OAI-PMH DublinCore
  • OAI-PMH DDI
Other Formats
  • JSON
  • BIBTEX

Confirm


Powered by WEKO3


Powered by WEKO3