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Structural model of...
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Rutsdottir, GudrunLund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
(författare)
Structural model of dodecameric heat-shock protein Hsp21 : Flexible N-terminal arms interact with client proteins while C-terminal tails maintain the dodecamer and chaperone activity
- Artikel/kapitelEngelska2017
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American Society for Biochemistry and Molecular Biology,2017
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printrdacarrier
Nummerbeteckningar
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LIBRIS-ID:oai:DiVA.org:kth-208817
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https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-208817URI
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https://doi.org/10.1074/jbc.M116.766816DOI
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https://lup.lub.lu.se/record/fcb8848a-4cf5-4dc1-84cc-6f1dc90a628dURI
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http://kipublications.ki.se/Default.aspx?queryparsed=id:135811905URI
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Språk:engelska
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Sammanfattning på:engelska
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Ämneskategori:ref swepub-contenttype
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Ämneskategori:art swepub-publicationtype
Anmärkningar
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QC 20170613
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Small heat-shock proteins (sHsps) prevent aggregation of thermosensitive client proteins in a first line of defense against cellular stress. The mechanisms by which they perform this function have been hard to define due to limited structural information; currently, there is only one high-resolution structure of a plant sHsp published, that of the cytosolic Hsp16.9. We took interest in Hsp21, a chloroplast-localized sHsp crucial for plant stress resistance, which has even longer N-terminal arms than Hsp16.9, with a functionally important and conserved methionine-rich motif. To provide a framework for investigating structure-function relationships of Hsp21 and understanding these sequence variations, we developed a structural model of Hsp21 based on homology modeling, cryo-EM, cross-linking mass spectrometry, NMR, and small-angle X-ray scattering. Our data suggest a dodecameric arrangement of two trimer-of-dimer discs stabilized by the C-terminal tails, possibly through tail-to-tail interactions between the discs, mediated through extended IXVXI motifs. Our model further suggests that six N-terminal arms are located on the outside of the dodecamer, accessible for interaction with client proteins, and distinct from previous undefined or inwardly facing arms. To test the importance of the IXVXI motif, we created the point mutant V181A, which, as expected, disrupts the Hsp21 dodecamer and decreases chaperone activity. Finally, our data emphasize that sHsp chaperone efficiency depends on oligomerization and that client interactions can occur both with and without oligomer dissociation. These results provide a generalizable workflow to explore sHsps, expand our understanding of sHsp structural motifs, and provide a testable Hsp21 structure model to inform future investigations.
Ämnesord och genrebeteckningar
Biuppslag (personer, institutioner, konferenser, titlar ...)
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Härmark, JohanKTH Royal Institute of Technology,KTH,Naturvetenskap och biomedicin,Karolinska Institutet, Sverige(Swepub:kth)u1hee262
(författare)
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Weide, YoranLund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)bioc-ywe
(författare)
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Hebert, HansKTH Royal Institute of Technology,KTH,Strukturell bioteknik,Karolinska Institutet, Sverige(Swepub:lu)mbfy-hhe
(författare)
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Rasmussen, Morten I.University of Southern Denmark
(författare)
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Wernersson, SvenLund University,Lunds universitet,Biofysikalisk kemi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biophysical Chemistry,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)sv0035we
(författare)
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Respondek, MichalLund University,Lunds universitet,Biofysikalisk kemi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biophysical Chemistry,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)bpc-mrn
(författare)
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Akke, MikaelLund University,Lunds universitet,Biofysikalisk kemi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biophysical Chemistry,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)fkm2-mak
(författare)
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Højrup, PeterUniversity of Southern Denmark
(författare)
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Koeck, Philip J. B.KTH Royal Institute of Technology,KTH,Strukturell bioteknik,Karolinska Institutet, Sverige(Swepub:kth)u1ikssgh
(författare)
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Söderberg, Christopher A.G.Lund University,Lunds universitet,MAX IV-laboratoriet,MAX IV Laboratory(Swepub:lu)mbfy-ces
(författare)
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Emanuelsson, CeciliaLund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)biok-cem
(författare)
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Biokemi och StrukturbiologiCentrum för Molekylär Proteinvetenskap
(creator_code:org_t)
Sammanhörande titlar
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Ingår i:Journal of Biological Chemistry: American Society for Biochemistry and Molecular Biology292:19, s. 8103-81210021-92581083-351X
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Rutsdottir, Gudr ...
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Härmark, Johan
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Weide, Yoran
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Hebert, Hans
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Rasmussen, Morte ...
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Wernersson, Sven
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Respondek, Micha ...
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Akke, Mikael
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Højrup, Peter
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Koeck, Philip J. ...
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Söderberg, Chris ...
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Emanuelsson, Cec ...
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