guest ::
| Home > Publications database > Direct observation of Hsp90-induced compaction in a protein chain. > print |
| Home > Publications database > Direct observation of Hsp90-induced compaction in a protein chain. > print |
| 001 | 182844 | ||
| 005 | 20240229145733.0 | ||
| 024 | 7 | _ | |a 10.1016/j.celrep.2022.111734 |2 doi |
| 024 | 7 | _ | |a pmid:36450251 |2 pmid |
| 024 | 7 | _ | |a 2211-1247 |2 ISSN |
| 024 | 7 | _ | |a 2639-1856 |2 ISSN |
| 024 | 7 | _ | |a altmetric:139360503 |2 altmetric |
| 037 | _ | _ | |a DKFZ-2022-02969 |
| 041 | _ | _ | |a English |
| 082 | _ | _ | |a 610 |
| 100 | 1 | _ | |a Mashaghi, Alireza |b 0 |
| 245 | _ | _ | |a Direct observation of Hsp90-induced compaction in a protein chain. |
| 260 | _ | _ | |a [New York, NY] |c 2022 |b Elsevier |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1669903821_15643 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 500 | _ | _ | |a DKFZ-ZMBH Alliance |
| 520 | _ | _ | |a The chaperone heat shock protein 90 (Hsp90) is well known to undergo important conformational changes, which depend on nucleotide and substrate interactions. Conversely, how the conformations of its unstable and disordered substrates are affected by Hsp90 is difficult to address experimentally yet is central to its function. Here, using optical tweezers, we find that Hsp90 promotes local contractions in unfolded chains that drive their global compaction down to dimensions of folded states. This compaction has a gradual nature while showing small steps, is stimulated by ATP, and performs mechanical work against counteracting forces that expand the chain dimensions. The Hsp90 interactions suppress the formation of larger-scale folded, misfolded, and aggregated structures. The observations support a model in which Hsp90 alters client conformations directly by promoting local intra-chain interactions while suppressing distant ones. We conjecture that chain compaction may be central to how Hsp90 protects unstable clients and cooperates with Hsp70. |
| 536 | _ | _ | |a 311 - Zellbiologie und Tumorbiologie (POF4-311) |0 G:(DE-HGF)POF4-311 |c POF4-311 |f POF IV |x 0 |
| 588 | _ | _ | |a Dataset connected to CrossRef, PubMed, , Journals: inrepo02.dkfz.de |
| 650 | _ | 7 | |a CP: Molecular biology |2 Other |
| 650 | _ | 7 | |a HSP90 |2 Other |
| 650 | _ | 7 | |a chaperone |2 Other |
| 650 | _ | 7 | |a conformational heterogeneity |2 Other |
| 650 | _ | 7 | |a optical tweezers |2 Other |
| 650 | _ | 7 | |a protein chain compaction |2 Other |
| 700 | 1 | _ | |a Moayed, Fatemeh |b 1 |
| 700 | 1 | _ | |a Koers, Eline J |b 2 |
| 700 | 1 | _ | |a Zheng, Yang |b 3 |
| 700 | 1 | _ | |a Till, Katharina |b 4 |
| 700 | 1 | _ | |a Kramer, Günter |0 P:(DE-He78)8b9aa336210db1592efa7400628e5a46 |b 5 |u dkfz |
| 700 | 1 | _ | |a Mayer, Matthias P |b 6 |
| 700 | 1 | _ | |a Tans, Sander J |b 7 |
| 773 | _ | _ | |a 10.1016/j.celrep.2022.111734 |g Vol. 41, no. 9, p. 111734 - |0 PERI:(DE-600)2649101-1 |n 9 |p 111734 |t Cell reports |v 41 |y 2022 |x 2211-1247 |
| 909 | C | O | |o oai:inrepo02.dkfz.de:182844 |p VDB |
| 910 | 1 | _ | |a Deutsches Krebsforschungszentrum |0 I:(DE-588b)2036810-0 |k DKFZ |b 5 |6 P:(DE-He78)8b9aa336210db1592efa7400628e5a46 |
| 913 | 1 | _ | |a DE-HGF |b Gesundheit |l Krebsforschung |1 G:(DE-HGF)POF4-310 |0 G:(DE-HGF)POF4-311 |3 G:(DE-HGF)POF4 |2 G:(DE-HGF)POF4-300 |4 G:(DE-HGF)POF |v Zellbiologie und Tumorbiologie |x 0 |
| 914 | 1 | _ | |y 2022 |
| 915 | _ | _ | |a Creative Commons Attribution-NonCommercial-NoDerivs CC BY-NC-ND (No Version) |0 LIC:(DE-HGF)CCBYNCNDNV |2 V:(DE-HGF) |b DOAJ |d 2021-02-03 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0160 |2 StatID |b Essential Science Indicators |d 2021-02-03 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)1190 |2 StatID |b Biological Abstracts |d 2021-02-03 |
| 915 | _ | _ | |a WoS |0 StatID:(DE-HGF)0113 |2 StatID |b Science Citation Index Expanded |d 2021-02-03 |
| 915 | _ | _ | |a Article Processing Charges |0 StatID:(DE-HGF)0561 |2 StatID |d 2021-02-03 |
| 915 | _ | _ | |a Fees |0 StatID:(DE-HGF)0700 |2 StatID |d 2021-02-03 |
| 915 | _ | _ | |a JCR |0 StatID:(DE-HGF)0100 |2 StatID |b CELL REP : 2021 |d 2022-11-17 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0200 |2 StatID |b SCOPUS |d 2022-11-17 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0300 |2 StatID |b Medline |d 2022-11-17 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0501 |2 StatID |b DOAJ Seal |d 2021-01-26T13:08:57Z |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0500 |2 StatID |b DOAJ |d 2021-01-26T13:08:57Z |
| 915 | _ | _ | |a Peer Review |0 StatID:(DE-HGF)0030 |2 StatID |b DOAJ : Blind peer review |d 2021-01-26T13:08:57Z |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0199 |2 StatID |b Clarivate Analytics Master Journal List |d 2022-11-17 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0150 |2 StatID |b Web of Science Core Collection |d 2022-11-17 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)1050 |2 StatID |b BIOSIS Previews |d 2022-11-17 |
| 915 | _ | _ | |a IF >= 5 |0 StatID:(DE-HGF)9905 |2 StatID |b CELL REP : 2021 |d 2022-11-17 |
| 920 | 1 | _ | |0 I:(DE-He78)A250-20160331 |k A250 |l A250 Chaperone und Proteasen |x 0 |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a I:(DE-He78)A250-20160331 |
| 980 | _ | _ | |a UNRESTRICTED |
| Library | Collection | CLSMajor | CLSMinor | Language | Author |
|---|