NMR characterization of the interaction of GroEL with amyloid β as a model ligand

Maho Yagi-Utsumi; Tomoko Kunihara; Takashi Nakamura; Yoshinori Uekusa; Koki Makabe; Kunihiro Kuwajima; Koichi Kato

doi:10.1016/j.febslet.2013.04.007

NMR characterization of the interaction of GroEL with amyloid β as a model ligand

Maho Yagi-Utsumi, Tomoko Kunihara, Takashi Nakamura, Yoshinori Uekusa, Koki Makabe, Kunihiro Kuwajima, Koichi Kato

Research output: Contribution to journal › Article › peer-review

20 Citations (Scopus)

Abstract

Here we report an NMR study on the substrate interaction modes of GroEL using amyloid β (Aβ) as a model ligand. We found that GroEL could suppress Aβ(1-40) amyloid formation by interacting with its two hydrophobic segments Leu17-Ala21 and Ala30-Val36, which involve key residues in fibril formation. The binding site of Aβ(1-40) was mapped on a pair of α-helices located in the GroEL apical domain. These results provide insights into chaperonin recognition of amyloidogenic proteins of pathological interest.

Original language	English
Pages (from-to)	1605-1609
Number of pages	5
Journal	FEBS Letters
Volume	587
Issue number	11
DOIs	https://doi.org/10.1016/j.febslet.2013.04.007
Publication status	Published - 2013 Jun 5
Externally published	Yes

Keywords

Amyloid β
Chaperonin
GroEL
NMR
NOE

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/j.febslet.2013.04.007

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title = "NMR characterization of the interaction of GroEL with amyloid β as a model ligand",

abstract = "Here we report an NMR study on the substrate interaction modes of GroEL using amyloid β (Aβ) as a model ligand. We found that GroEL could suppress Aβ(1-40) amyloid formation by interacting with its two hydrophobic segments Leu17-Ala21 and Ala30-Val36, which involve key residues in fibril formation. The binding site of Aβ(1-40) was mapped on a pair of α-helices located in the GroEL apical domain. These results provide insights into chaperonin recognition of amyloidogenic proteins of pathological interest.",

keywords = "Amyloid β, Chaperonin, GroEL, NMR, NOE",

author = "Maho Yagi-Utsumi and Tomoko Kunihara and Takashi Nakamura and Yoshinori Uekusa and Koki Makabe and Kunihiro Kuwajima and Koichi Kato",

note = "Funding Information: We thank Ms. Hiroko Mizuki ( National Institute of Natural Sciences ), Ms. Kiyomi Senda, and Ms. Kumiko Hattori ( Nagoya City University ) for their help with the preparation of recombinant proteins. This work was supported in part by Grants-in-Aid for Scientific Research on Innovative Areas ( 20107004 , 20107009 ) and for Research Activity Start-up ( 23870043 ) from the Ministry of Education, Culture, Sports, Science and Technology of Japan and Research Funding for Longevity Sciences ( 22-14 ) from the National Center for Geriatrics and Gerontology, Japan . ",

year = "2013",

month = jun,

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doi = "10.1016/j.febslet.2013.04.007",

language = "English",

volume = "587",

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T1 - NMR characterization of the interaction of GroEL with amyloid β as a model ligand

AU - Yagi-Utsumi, Maho

AU - Kunihara, Tomoko

AU - Nakamura, Takashi

AU - Uekusa, Yoshinori

AU - Makabe, Koki

AU - Kuwajima, Kunihiro

AU - Kato, Koichi

N1 - Funding Information: We thank Ms. Hiroko Mizuki ( National Institute of Natural Sciences ), Ms. Kiyomi Senda, and Ms. Kumiko Hattori ( Nagoya City University ) for their help with the preparation of recombinant proteins. This work was supported in part by Grants-in-Aid for Scientific Research on Innovative Areas ( 20107004 , 20107009 ) and for Research Activity Start-up ( 23870043 ) from the Ministry of Education, Culture, Sports, Science and Technology of Japan and Research Funding for Longevity Sciences ( 22-14 ) from the National Center for Geriatrics and Gerontology, Japan .

PY - 2013/6/5

Y1 - 2013/6/5

N2 - Here we report an NMR study on the substrate interaction modes of GroEL using amyloid β (Aβ) as a model ligand. We found that GroEL could suppress Aβ(1-40) amyloid formation by interacting with its two hydrophobic segments Leu17-Ala21 and Ala30-Val36, which involve key residues in fibril formation. The binding site of Aβ(1-40) was mapped on a pair of α-helices located in the GroEL apical domain. These results provide insights into chaperonin recognition of amyloidogenic proteins of pathological interest.

AB - Here we report an NMR study on the substrate interaction modes of GroEL using amyloid β (Aβ) as a model ligand. We found that GroEL could suppress Aβ(1-40) amyloid formation by interacting with its two hydrophobic segments Leu17-Ala21 and Ala30-Val36, which involve key residues in fibril formation. The binding site of Aβ(1-40) was mapped on a pair of α-helices located in the GroEL apical domain. These results provide insights into chaperonin recognition of amyloidogenic proteins of pathological interest.

KW - Amyloid β

KW - Chaperonin

KW - GroEL

KW - NMR

KW - NOE

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SN - 0014-5793

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SP - 1605

EP - 1609

JO - FEBS Letters

JF - FEBS Letters

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ER -

NMR characterization of the interaction of GroEL with amyloid β as a model ligand

Abstract

Keywords

ASJC Scopus subject areas

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