{"file":[{"creator":"cchlebak","file_name":"2021_FrontiersMolBioSc_Sučec.pdf","access_level":"open_access","checksum":"a5c9dbf80dc2c5aaa737f456c941d964","date_updated":"2021-11-23T15:06:58Z","file_id":"10333","relation":"main_file","success":1,"file_size":4700798,"date_created":"2021-11-23T15:06:58Z","content_type":"application/pdf"}],"acknowledgement":"We thank Juan C. Fontecilla-Camps for insightful discussions related to ATP-driven machineries, and Elif Karagöz for providing the structural model of the Hsp90-Tau complex. This study was supported by the European Research Council (StG-2012-311318-ProtDyn2Function) and the Agence Nationale de la Recherche (ANR-18-CE92-0032-MitoMemProtImp).","doi":"10.3389/fmolb.2021.762005","publication":"Frontiers in Molecular Biosciences","_id":"10323","article_number":"762005","date_updated":"2023-08-14T11:55:04Z","oa":1,"language":[{"iso":"eng"}],"day":"25","year":"2021","publisher":"Frontiers","volume":8,"external_id":{"isi":["000717241700001"],"pmid":["34760928"]},"publication_status":"published","department":[{"_id":"PaSc"}],"citation":{"ieee":"I. Sučec, B. Bersch, and P. Schanda, “How do chaperones bind (partly) unfolded client proteins?,” <i>Frontiers in Molecular Biosciences</i>, vol. 8. Frontiers, 2021.","apa":"Sučec, I., Bersch, B., &#38; Schanda, P. (2021). How do chaperones bind (partly) unfolded client proteins? <i>Frontiers in Molecular Biosciences</i>. Frontiers. <a href=\"https://doi.org/10.3389/fmolb.2021.762005\">https://doi.org/10.3389/fmolb.2021.762005</a>","mla":"Sučec, Iva, et al. “How Do Chaperones Bind (Partly) Unfolded Client Proteins?” <i>Frontiers in Molecular Biosciences</i>, vol. 8, 762005, Frontiers, 2021, doi:<a href=\"https://doi.org/10.3389/fmolb.2021.762005\">10.3389/fmolb.2021.762005</a>.","chicago":"Sučec, Iva, Beate Bersch, and Paul Schanda. “How Do Chaperones Bind (Partly) Unfolded Client Proteins?” <i>Frontiers in Molecular Biosciences</i>. Frontiers, 2021. <a href=\"https://doi.org/10.3389/fmolb.2021.762005\">https://doi.org/10.3389/fmolb.2021.762005</a>.","short":"I. Sučec, B. Bersch, P. Schanda, Frontiers in Molecular Biosciences 8 (2021).","ama":"Sučec I, Bersch B, Schanda P. How do chaperones bind (partly) unfolded client proteins? <i>Frontiers in Molecular Biosciences</i>. 2021;8. doi:<a href=\"https://doi.org/10.3389/fmolb.2021.762005\">10.3389/fmolb.2021.762005</a>","ista":"Sučec I, Bersch B, Schanda P. 2021. How do chaperones bind (partly) unfolded client proteins? Frontiers in Molecular Biosciences. 8, 762005."},"intvolume":"         8","author":[{"last_name":"Sučec","full_name":"Sučec, Iva","first_name":"Iva"},{"first_name":"Beate","full_name":"Bersch, Beate","last_name":"Bersch"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","first_name":"Paul","last_name":"Schanda","full_name":"Schanda, Paul"}],"isi":1,"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"},"abstract":[{"lang":"eng","text":"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."}],"pmid":1,"quality_controlled":"1","scopus_import":"1","article_type":"original","has_accepted_license":"1","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","article_processing_charge":"Yes (via OA deal)","date_published":"2021-10-25T00:00:00Z","file_date_updated":"2021-11-23T15:06:58Z","oa_version":"Published Version","date_created":"2021-11-21T23:01:29Z","month":"10","publication_identifier":{"eissn":["2296-889X"]},"type":"journal_article","ddc":["547"],"title":"How do chaperones bind (partly) unfolded client proteins?","status":"public"}