Conformation of Amyloid Fibrils of β2-Microglobulin Probed by Tryptophan Mutagenesis

Kihara, Miho; Chatani, Eri; Iwata, Kentaro; Yamamoto, Kaori; Matsuura, Takanori; Nakagawa, Atsushi; Naiki, Hironobu; Goto, Yuji

doi:https://doi.org/10.1074/jbc.M605358200

アクセス数:251件（2025-01-14 02:19 集計）

固定URL: https://hdl.handle.net/11094/71292

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タイトル	Conformation of Amyloid Fibrils of β2-Microglobulin Probed by Tryptophan Mutagenesis
著者	著者名 Kihara, Miho
	NRID 1000000432493 1000000432493 著者名 Chatani, Eri
	著者名 Iwata, Kentaro
	著者名 Yamamoto, Kaori
	著者名 Matsuura, Takanori
	NRID 1000020188890 1000020188890 ORCID 0000-0002-1700-7861 0000-0002-1700-7861 researchmap permalink atsushi_nakagawa atsushi_nakagawa Scopus Author ID 7202934909 7202934909 著者名 Nakagawa, Atsushi
	NRID 1000010227704 1000010227704 著者名 Naiki, Hironobu
	NRID 1000040153770 1000040153770 researchmap permalink read0014440 read0014440 著者名 Goto, Yuji
内容	This research was originally published in the Journal of Biological Chemistry. Miho Kihara, Eri Chatani, Kentaro Iwata, Kaori Yamamoto, Takanori Matsuura, Atsushi Nakagawa, Hironobu Naiki and Yuji Goto. Conformation of Amyloid Fibrils of β2-Microglobulin Probed by Tryptophan Mutagenesis. J. Biol. Chem. 2006; 281, 31061–31069. © the American Society for Biochemistry and Molecular Biology
抄録	β2-Microglobulin (β2-m), a protein responsible for dialysis-related amyloidosis, adopts an immunoglobulin domain fold in its native state. Although β2-m has Trp residues at positions 60 and 95, both are located near the surface of the domain. Hence, β2-m does not have a conserved Trp common to other immunoglobulin domains, which is buried in close proximity to the disulfide bond. To study the structure of amyloid fibrils in relation to their native fold, we prepared a series of Trp mutants. Trp60 and Trp95 were both replaced with Phe, and a single Trp was introduced at various positions. Among various mutants, W39-β2-m, in which a Trp was introduced at the position corresponding to the conserved Trp, exhibited a remarkable quenching of fluorescence in the native state, as observed for other immunoglobulin domains. An x-ray structural analysis revealed that W39-β2-m assumes the native fold with Trp39 located in the vicinity of the disulfide bond. Comparison of the fluorescence spectra of various mutants for the native and fibrillar forms indicated that, while the Trp residues introduced in the middle of the β2-m sequence tend to be buried in the fibrils, those located in the C-terminal region are more exposed. In addition, the fluorescence spectra of fibrils prepared at pH 2.5 and 7.0 revealed a large difference in the fluorescence intensity for W60-β2-m, implying a major structural difference between them.
出版者	American Society for Biochemistry and Molecular Biology
収録物名	Journal of Biological Chemistry
巻(号)	281(41)
ページ	31061-31069
刊行年月	2006-10
言語	英語
ハンドルURL	https://hdl.handle.net/11094/71292
eISSN	1083351X
NCID	AA1202461X
関連情報 (isIdenticalTo)	DOI (出版社版) https://doi.org/10.1074/jbc.M605358200
アクセス権	open access
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	Journal of Biological Chemistry. 2006, 281(41), p. 31061-31069
DC.title	Conformation of Amyloid Fibrils of β2-Microglobulin Probed by Tryptophan Mutagenesis
DC.creator	Kihara, Miho
	Chatani, Eri
	Iwata, Kentaro
	Yamamoto, Kaori
	Matsuura, Takanori
	Nakagawa, Atsushi
	Naiki, Hironobu
	Goto, Yuji
DC.publisher	American Society for Biochemistry and Molecular Biology
DC.language' scheme='DCTERMS.RFC1766	英語
DC.type' scheme='DCTERMS.DCMIType	text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2006-10
DC.identifier	https://doi.org/10.1074/jbc.M605358200
DC.description	This research was originally published in the Journal of Biological Chemistry. Miho Kihara, Eri Chatani, Kentaro Iwata, Kaori Yamamoto, Takanori Matsuura, Atsushi Nakagawa, Hironobu Naiki and Yuji Goto. Conformation of Amyloid Fibrils of β2-Microglobulin Probed by Tryptophan Mutagenesis. J. Biol. Chem. 2006; 281, 31061–31069. © the American Society for Biochemistry and Molecular Biology
DCTERMS.abstract	β2-Microglobulin (β2-m), a protein responsible for dialysis-related amyloidosis, adopts an immunoglobulin domain fold in its native state. Although β2-m has Trp residues at positions 60 and 95, both are located near the surface of the domain. Hence, β2-m does not have a conserved Trp common to other immunoglobulin domains, which is buried in close proximity to the disulfide bond. To study the structure of amyloid fibrils in relation to their native fold, we prepared a series of Trp mutants. Trp60 and Trp95 were both replaced with Phe, and a single Trp was introduced at various positions. Among various mutants, W39-β2-m, in which a Trp was introduced at the position corresponding to the conserved Trp, exhibited a remarkable quenching of fluorescence in the native state, as observed for other immunoglobulin domains. An x-ray structural analysis revealed that W39-β2-m assumes the native fold with Trp39 located in the vicinity of the disulfide bond. Comparison of the fluorescence spectra of various mutants for the native and fibrillar forms indicated that, while the Trp residues introduced in the middle of the β2-m sequence tend to be buried in the fibrils, those located in the C-terminal region are more exposed. In addition, the fluorescence spectra of fibrils prepared at pH 2.5 and 7.0 revealed a large difference in the fluorescence intensity for W60-β2-m, implying a major structural difference between them.
DC.format	71292
citation_title	Conformation of Amyloid Fibrils of β2-Microglobulin Probed by Tryptophan Mutagenesis
citation_author	Kihara, Miho
	Chatani, Eri
	Iwata, Kentaro
	Yamamoto, Kaori
	Matsuura, Takanori
	Nakagawa, Atsushi
	Naiki, Hironobu
	Goto, Yuji
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	英語
citation_date	2006-10
citation_journal_title	Journal of Biological Chemistry
citation_volume	281
citation_issue	41
citation_firstpage	31061
citation_lastpage	31069
citation_doi	https://doi.org/10.1074/jbc.M605358200
citation_public_url	https://hdl.handle.net/11094/71292

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