Interaction of β-lactoglobulin with chaperonin GroEL

Sakai, Kazuko; Hoshino, Masaru; Goto, Yuji

アクセス数:130件（2024-11-09 08:20 集計）

固定URL: https://hdl.handle.net/11094/71264

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タイトル	Interaction of β-lactoglobulin with chaperonin GroEL
著者	著者名 Sakai, Kazuko
	NRID 1000070304053 1000070304053 著者名 Hoshino, Masaru
	NRID 1000040153770 1000040153770 researchmap permalink read0014440 read0014440 著者名 Goto, Yuji
キーワード等	β-Lactoglobulin
	GroEL
	Protein Folding
	Substrate Recognition
	Salt Effects
	Hydrophobic Interaction
内容	Sakai, Kazuko, Hoshino, Masaru and Goto, Yuji "Interaction of β-lactoglobulin with chaperonin GroEL", Proceedings of the Indian National Science Academy, 68, 4A, 341-347, Indian National Science Academy, 2002
抄録	The roles of electrostatic and hydrophobic interactions in the substrate recognition of GroEL were studied with bovine β-lactoglobulin as a substrate. We previously reported that, although the native state of β-lactoglobulin does not interact with GroEL, the modified protein in which the two disulfide bonds were reduced formed a stable complex. To clarify the extent of denaturation necessary for the interaction, we examined the interaction of GroEL with the intermediate state of β-lactoglobulin in which the free thiol group was specifically modified with 5,5' -dithiobis (2-nitrobenzoic acid). The thiol-modified β-lactoglobulin formed a complex with GroEL as measured by size-exclusion chromatography, indicating that moderate denaturation is enough for the interaction. We then measured the interaction between GroEL and the refolding intermediate of the disulfide intact β-lactoglobulin. Although the interaction was marginal under low salt conditions, notable interaction was observed by the addition of KCI. Since pl values of GroEL and β-lactoglobulin are 4.7 and 4.5, respectively, the addition of salt was considered to shield the unfavourable charge repulsion. Tryptophyl fluorescence of the kinetic intermediate indicated that tryptophan residues were buried upon binding. These results confirmed the previous view that suppression of the unfavourable electrostatic repulsion in addition to exertion of favourable hydrophobic interaction is important for the binding of substrate proteins to GroEL.
出版者	Indian National Science Academy
収録物名	Proceedings of the Indian National Science Academy
巻(号)	68(4A)
ページ	341-347
刊行年月	2002-07
言語	英語
ハンドルURL	https://hdl.handle.net/11094/71264
PISSN	03700046
NCID	AA12158303
アクセス権	open access
権利情報	This article is licensed under a Creative Commons Attribution 4.0 International License.
出版タイプ	Version of Record
カテゴリ	学術雑誌論文 Journal Article

資源タイプ	学術雑誌論文
ローカル資源タイプ	学術雑誌論文
DCMI資源タイプ	text
DCTERMS.bibliographicCitation	Proceedings of the Indian National Science Academy. 2002, 68(4A), p. 341-347
DC.title	Interaction of β-lactoglobulin with chaperonin GroEL
DC.creator	Sakai, Kazuko
	Hoshino, Masaru
	Goto, Yuji
DC.publisher	Indian National Science Academy
DC.language' scheme='DCTERMS.RFC1766	英語
DC.type' scheme='DCTERMS.DCMIType	text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2002-07
DC.subject	β-Lactoglobulin
	GroEL
	Protein Folding
	Substrate Recognition
	Salt Effects
	Hydrophobic Interaction
DC.description	Sakai, Kazuko, Hoshino, Masaru and Goto, Yuji "Interaction of β-lactoglobulin with chaperonin GroEL", Proceedings of the Indian National Science Academy, 68, 4A, 341-347, Indian National Science Academy, 2002
DCTERMS.abstract	The roles of electrostatic and hydrophobic interactions in the substrate recognition of GroEL were studied with bovine β-lactoglobulin as a substrate. We previously reported that, although the native state of β-lactoglobulin does not interact with GroEL, the modified protein in which the two disulfide bonds were reduced formed a stable complex. To clarify the extent of denaturation necessary for the interaction, we examined the interaction of GroEL with the intermediate state of β-lactoglobulin in which the free thiol group was specifically modified with 5,5' -dithiobis (2-nitrobenzoic acid). The thiol-modified β-lactoglobulin formed a complex with GroEL as measured by size-exclusion chromatography, indicating that moderate denaturation is enough for the interaction. We then measured the interaction between GroEL and the refolding intermediate of the disulfide intact β-lactoglobulin. Although the interaction was marginal under low salt conditions, notable interaction was observed by the addition of KCI. Since pl values of GroEL and β-lactoglobulin are 4.7 and 4.5, respectively, the addition of salt was considered to shield the unfavourable charge repulsion. Tryptophyl fluorescence of the kinetic intermediate indicated that tryptophan residues were buried upon binding. These results confirmed the previous view that suppression of the unfavourable electrostatic repulsion in addition to exertion of favourable hydrophobic interaction is important for the binding of substrate proteins to GroEL.
DC.rights	This article is licensed under a Creative Commons Attribution 4.0 International License.
DC.format	71264
citation_title	Interaction of β-lactoglobulin with chaperonin GroEL
citation_author	Sakai, Kazuko
	Hoshino, Masaru
	Goto, Yuji
citation_publisher	Indian National Science Academy
citation_language	英語
citation_date	2002-07
citation_journal_title	Proceedings of the Indian National Science Academy
citation_volume	68
citation_issue	4A
citation_firstpage	341
citation_lastpage	347
citation_public_url	https://hdl.handle.net/11094/71264

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