Academic Journal
How do Chaperones Bind (Partly) Unfolded Client Proteins?
| العنوان: | How do Chaperones Bind (Partly) Unfolded Client Proteins? |
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| المؤلفون: | Sučec, Iva, Bersch, Beate, Schanda, Paul |
| المساهمون: | Institut de biologie structurale (IBS - UMR 5075), Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA), Institute of Science and Technology Klosterneuburg, Austria (IST Austria), ANR-18-CE92-0032,MitoMemProtImp,Etudes structurales et fonctionnelles de l'import et le transfert à travers l'espace inter-membranaire des protéines membranaires mitochondriales(2018), European Project: 311318,EC:FP7:ERC,ERC-2012-StG_20111109,PROTDYN2FUNCTION(2013) |
| المصدر: | ISSN: 2296-889X ; Frontiers in Molecular Biosciences ; https://hal.science/hal-03408836 ; Frontiers in Molecular Biosciences, 2021, 8, pp.762005. ⟨10.3389/fmolb.2021.762005⟩ ; https://www.frontiersin.org/articles/10.3389/fmolb.2021.762005/full. |
| بيانات النشر: | CCSD Frontiers Media |
| سنة النشر: | 2021 |
| المجموعة: | Université Grenoble Alpes: HAL |
| مصطلحات موضوعية: | [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM] |
| الوصف: | International audience ; Molecular chaperones are central to cellular protein homeostasis. Dynamic disorder is a key feature of the complexes of molecular chaperones and their client proteins, and it facilitates the client release towards a folded state or the handover to downstream components. The dynamic nature also implies that a given chaperone can interact with many different client proteins, based on physico-chemical sequence properties rather than on structural complementarity of their (folded) 3D structure. Yet, the balance between this promiscuity and some degree of client specificity is poorly understood. Here, we review recent atomic-level descriptions of chaperones with client proteins, including chaperones in complex with intrinsically disordered proteins, with membrane-protein precursors, or partially folded client proteins. We focus hereby on chaperone-client interactions that are independent of ATP. The picture emerging from these studies highlights the importance of dynamics in these complexes, whereby several interaction types, not only hydrophobic ones, contribute to the complex formation. We discuss these features of chaperone-client complexes and possible factors that may contribute to this balance of promiscuity and specificity. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| Relation: | info:eu-repo/grantAgreement/EC/FP7/311318/EU/Functional protein dynamics studied by solution- and solid-state NMR spectroscopy/PROTDYN2FUNCTION |
| DOI: | 10.3389/fmolb.2021.762005 |
| الاتاحة: | https://hal.science/hal-03408836 https://hal.science/hal-03408836v1/document https://hal.science/hal-03408836v1/file/su1.pdf https://doi.org/10.3389/fmolb.2021.762005 |
| Rights: | info:eu-repo/semantics/OpenAccess |
| رقم الانضمام: | edsbas.E0273C55 |
| قاعدة البيانات: | BASE |
| DOI: | 10.3389/fmolb.2021.762005 |
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