The anti-aggregation holdase Hsp33 promotes the formation of folded protein structures
Holdase chaperones are known to be central to suppressing aggregation, but how they affect substrate conformations remains poorly understood. Here, we use optical tweezers to study how the holdase Hsp33 alters folding transitions within single maltose binding proteins and aggregation transitions bet...
Gespeichert in:
| Hauptverfasser: | , , |
|---|---|
| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
2020
|
| In: |
Biophysical journal
Year: 2020, Jahrgang: 118, Heft: 1, Pages: 85-95 |
| ISSN: | 1542-0086 |
| DOI: | 10.1016/j.bpj.2019.10.040 |
| Online-Zugang: | Verlag, Volltext: https://doi.org/10.1016/j.bpj.2019.10.040 Verlag, Volltext: http://www.sciencedirect.com/science/article/pii/S000634951930904X 
|
| Verfasserangaben: | Fatemeh Moayed, Sergey Bezrukavnikov, Mohsin M. Naqvi, Bastian Groitl, Claudia M. Cremers, Guenter Kramer, Kingshuk Ghosh, Ursula Jakob, Sander J. Tans |
MARC
| LEADER | 00000caa a2200000 c 4500 | ||
|---|---|---|---|
| 001 | 168922150X | ||
| 003 | DE-627 | ||
| 005 | 20220817222205.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 200204s2020 xx |||||o 00| ||eng c | ||
| 024 | 7 | |a 10.1016/j.bpj.2019.10.040 |2 doi | |
| 035 | |a (DE-627)168922150X | ||
| 035 | |a (DE-599)KXP168922150X | ||
| 035 | |a (OCoLC)1341303552 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rda | ||
| 041 | |a eng | ||
| 084 | |a 32 |2 sdnb | ||
| 100 | 1 | |a Moayed, Fatemeh |e VerfasserIn |0 (DE-588)1204088489 |0 (DE-627)1689220872 |4 aut | |
| 245 | 1 | 4 | |a The anti-aggregation holdase Hsp33 promotes the formation of folded protein structures |c Fatemeh Moayed, Sergey Bezrukavnikov, Mohsin M. Naqvi, Bastian Groitl, Claudia M. Cremers, Guenter Kramer, Kingshuk Ghosh, Ursula Jakob, Sander J. Tans |
| 264 | 1 | |c 2020 | |
| 300 | |a 11 | ||
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a Computermedien |b c |2 rdamedia | ||
| 338 | |a Online-Ressource |b cr |2 rdacarrier | ||
| 500 | |a Available online 11 November 2019 | ||
| 500 | |a Gesehen am 04.02.2020 | ||
| 520 | |a Holdase chaperones are known to be central to suppressing aggregation, but how they affect substrate conformations remains poorly understood. Here, we use optical tweezers to study how the holdase Hsp33 alters folding transitions within single maltose binding proteins and aggregation transitions between maltose binding protein substrates. Surprisingly, we find that Hsp33 not only suppresses aggregation but also guides the folding process. Two modes of action underlie these effects. First, Hsp33 binds unfolded chains, which suppresses aggregation between substrates and folding transitions within substrates. Second, Hsp33 binding promotes substrate states in which most of the chain is folded and modifies their structure, possibly by intercalating its intrinsically disordered regions. A statistical ensemble model shows how Hsp33 function results from the competition between these two contrasting effects. Our findings reveal an unexpectedly comprehensive functional repertoire for Hsp33 that may be more prevalent among holdases and dispels the notion of a strict chaperone hierarchy. | ||
| 700 | 1 | |a Bezrukavnikov, Sergey |e VerfasserIn |0 (DE-588)120408873X |0 (DE-627)1689221135 |4 aut | |
| 700 | 1 | |a Kramer, Günter |e VerfasserIn |0 (DE-588)1060239582 |0 (DE-627)799340294 |0 (DE-576)416341136 |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Biophysical journal |d Cambridge, Mass. : Cell Press, 1960 |g 118(2020), 1, Seite 85-95 |h Online-Ressource |w (DE-627)270425357 |w (DE-600)1477214-0 |w (DE-576)091017602 |x 1542-0086 |7 nnas |a The anti-aggregation holdase Hsp33 promotes the formation of folded protein structures |
| 773 | 1 | 8 | |g volume:118 |g year:2020 |g number:1 |g pages:85-95 |g extent:11 |a The anti-aggregation holdase Hsp33 promotes the formation of folded protein structures |
| 856 | 4 | 0 | |u https://doi.org/10.1016/j.bpj.2019.10.040 |x Verlag |x Resolving-System |3 Volltext |
| 856 | 4 | 0 | |u http://www.sciencedirect.com/science/article/pii/S000634951930904X |x Verlag |x Resolving-System |3 Volltext |
| 951 | |a AR | ||
| 992 | |a 20200204 | ||
| 993 | |a Article | ||
| 994 | |a 2020 | ||
| 998 | |g 1060239582 |a Kramer, Günter |m 1060239582:Kramer, Günter |d 700000 |d 706000 |e 700000PK1060239582 |e 706000PK1060239582 |k 0/700000/ |k 1/700000/706000/ |p 6 | ||
| 999 | |a KXP-PPN168922150X |e 3587313881 | ||
| BIB | |a Y | ||
| SER | |a journal | ||
| JSO | |a {"title":[{"title":"The anti-aggregation holdase Hsp33 promotes the formation of folded protein structures","title_sort":"anti-aggregation holdase Hsp33 promotes the formation of folded protein structures"}],"physDesc":[{"extent":"11 S."}],"relHost":[{"physDesc":[{"extent":"Online-Ressource"}],"part":{"text":"118(2020), 1, Seite 85-95","volume":"118","pages":"85-95","year":"2020","issue":"1","extent":"11"},"language":["eng"],"type":{"bibl":"periodical","media":"Online-Ressource"},"recId":"270425357","name":{"displayForm":["ed. by the Biophysical Society"]},"title":[{"title":"Biophysical journal","title_sort":"Biophysical journal","subtitle":"BJ"}],"titleAlt":[{"title":"BJ"}],"note":["Gesehen am 20.05.2020"],"pubHistory":["1.1960/61 -"],"id":{"issn":["1542-0086"],"eki":["270425357"],"zdb":["1477214-0"]},"corporate":[{"display":"Biophysical Society","role":"isb"}],"origin":[{"dateIssuedKey":"1960","publisherPlace":"Cambridge, Mass. ; Bethesda, Md. ; New York, NY","dateIssuedDisp":"1960-","publisher":"Cell Press ; Soc. ; Rockefeller Univ. Press"}],"disp":"The anti-aggregation holdase Hsp33 promotes the formation of folded protein structuresBiophysical journal"}],"origin":[{"dateIssuedKey":"2020","dateIssuedDisp":"2020"}],"name":{"displayForm":["Fatemeh Moayed, Sergey Bezrukavnikov, Mohsin M. Naqvi, Bastian Groitl, Claudia M. Cremers, Guenter Kramer, Kingshuk Ghosh, Ursula Jakob, Sander J. Tans"]},"type":{"media":"Online-Ressource","bibl":"article-journal"},"id":{"doi":["10.1016/j.bpj.2019.10.040"],"eki":["168922150X"]},"recId":"168922150X","person":[{"given":"Fatemeh","display":"Moayed, Fatemeh","role":"aut","family":"Moayed"},{"display":"Bezrukavnikov, Sergey","role":"aut","family":"Bezrukavnikov","given":"Sergey"},{"given":"Günter","display":"Kramer, Günter","role":"aut","family":"Kramer"}],"language":["eng"],"note":["Available online 11 November 2019","Gesehen am 04.02.2020"]} | ||
| SRT | |a MOAYEDFATEANTIAGGREG2020 | ||