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Short hydrophobic l...
Short hydrophobic loop motifs in BRICHOS domains determine chaperone activity against amorphous protein aggregation but not against amyloid formation
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- Chen, Gefei (author)
- Karolinska Inst, Dept Biosci & Nutr, S-14183 Huddinge, Sweden.
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- Leppert, Axel (author)
- Karolinska Inst, Dept Biosci & Nutr, S-14183 Huddinge, Sweden.;Karolinska Inst, Dept Microbiol Tumour & Cell Biol, S-17165 Solna, Sweden.
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- Poska, Helen (author)
- Karolinska Inst, Dept Biosci & Nutr, S-14183 Huddinge, Sweden.;Tallinn Univ, Sch Nat Sci & Hlth, Tallinn, Estonia.
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- Nilsson, Harriet (author)
- KTH,Strukturell bioteknik
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- Alvira, Carlos Piedrafita (author)
- Karolinska Inst, Dept Biosci & Nutr, S-14183 Huddinge, Sweden.
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- Zhong, Xueying (author)
- KTH,Strukturell bioteknik
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- Koeck, Philip J. B. (author)
- Karolinska Institutet,KTH,Strukturell bioteknik
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- Jegerschöld, Caroline (author)
- KTH,Strukturell bioteknik
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- Abelein, Axel (author)
- Karolinska Institutet
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- Hebert, Hans (author)
- KTH,Strukturell bioteknik
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- Johansson, Jan (author)
- Karolinska Inst, Dept Biosci & Nutr, S-14183 Huddinge, Sweden.
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Karolinska Inst, Dept Biosci & Nutr, S-14183 Huddinge, Sweden Karolinska Inst, Dept Biosci & Nutr, S-14183 Huddinge, Sweden.;Karolinska Inst, Dept Microbiol Tumour & Cell Biol, S-17165 Solna, Sweden. (creator_code:org_t)
- Springer Nature, 2023
- 2023
- English.
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In: Communications Biology. - : Springer Nature. - 2399-3642. ; 6:1
- Related links:
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https://doi.org/10.1...
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https://urn.kb.se/re...
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Abstract
Subject headings
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- BRICHOS domain oligomerization exposes three short hydrophobic motifs that are necessary for efficient chaperone activity against amorphous protein aggregation. ATP-independent molecular chaperones are important for maintaining cellular fitness but the molecular determinants for preventing aggregation of partly unfolded protein substrates remain unclear, particularly regarding assembly state and basis for substrate recognition. The BRICHOS domain can perform small heat shock (sHSP)-like chaperone functions to widely different degrees depending on its assembly state and sequence. Here, we observed three hydrophobic sequence motifs in chaperone-active domains, and found that they get surface-exposed when the BRICHOS domain assembles into larger oligomers. Studies of loop-swap variants and site-specific mutants further revealed that the biological hydrophobicities of the three short motifs linearly correlate with the efficiency to prevent amorphous protein aggregation. At the same time, they do not at all correlate with the ability to prevent ordered amyloid fibril formation. The linear correlations also accurately predict activities of chimeras containing short hydrophobic sequence motifs from a sHSP that is unrelated to BRICHOS. Our data indicate that short, exposed hydrophobic motifs brought together by oligomerisation are sufficient and necessary for efficient chaperone activity against amorphous protein aggregation.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Publication and Content Type
- ref (subject category)
- art (subject category)
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- By the author/editor
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Chen, Gefei
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Leppert, Axel
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Poska, Helen
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Nilsson, Harriet
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Alvira, Carlos P ...
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Zhong, Xueying
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show more...
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Koeck, Philip J. ...
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Jegerschöld, Car ...
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Abelein, Axel
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Hebert, Hans
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Johansson, Jan
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- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Biochemistry and ...
- Articles in the publication
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Communications B ...
- By the university
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Royal Institute of Technology
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Karolinska Institutet