{"pmid":1,"article_type":"original","publisher":"American Association for the Advancement of Science","license":"https://creativecommons.org/licenses/by/4.0/","scopus_import":"1","article_processing_charge":"Yes","quality_controlled":"1","title":"Protein chain collapse modulation and folding stimulation by GroEL-ES","issue":"9","author":[{"last_name":"Naqvi","full_name":"Naqvi, Mohsin M.","first_name":"Mohsin M."},{"full_name":"Avellaneda Sarrió, Mario","first_name":"Mario","orcid":"0000-0001-6406-524X","last_name":"Avellaneda Sarrió","id":"DC4BA84C-56E6-11EA-AD5D-348C3DDC885E"},{"full_name":"Roth, Andrew","first_name":"Andrew","last_name":"Roth"},{"full_name":"Koers, Eline J.","first_name":"Eline J.","last_name":"Koers"},{"last_name":"Roland","full_name":"Roland, Antoine","first_name":"Antoine"},{"last_name":"Sunderlikova","first_name":"Vanda","full_name":"Sunderlikova, Vanda"},{"full_name":"Kramer, Günter","first_name":"Günter","last_name":"Kramer"},{"first_name":"Hays S.","full_name":"Rye, Hays S.","last_name":"Rye"},{"first_name":"Sander J.","full_name":"Tans, Sander J.","last_name":"Tans"}],"external_id":{"pmid":["35245117"]},"_id":"17072","abstract":[{"text":"<jats:p>The collapse of polypeptides is thought important to protein folding, aggregation, intrinsic disorder, and phase separation. However, whether polypeptide collapse is modulated in cells to control protein states is unclear. Here, using integrated protein manipulation and imaging, we show that the chaperonin GroEL-ES can accelerate the folding of proteins by strengthening their collapse. GroEL induces contractile forces in substrate chains, which draws them into the cavity and triggers a general compaction and discrete folding transitions, even for slow-folding proteins. This collapse enhancement is strongest in the nucleotide-bound states of GroEL and is aided by GroES binding to the cavity rim and by the amphiphilic C-terminal tails at the cavity bottom. Collapse modulation is distinct from other proposed GroEL-ES folding acceleration mechanisms, including steric confinement and misfold unfolding. Given the prevalence of collapse throughout the proteome, we conjecture that collapse modulation is more generally relevant within the protein quality control machinery.</jats:p>","lang":"eng"}],"ddc":["570"],"oa_version":"Published Version","citation":{"ama":"Naqvi MM, Avellaneda Sarrió M, Roth A, et al. Protein chain collapse modulation and folding stimulation by GroEL-ES. <i>Science Advances</i>. 2022;8(9). doi:<a href=\"https://doi.org/10.1126/sciadv.abl6293\">10.1126/sciadv.abl6293</a>","apa":"Naqvi, M. M., Avellaneda Sarrió, M., Roth, A., Koers, E. J., Roland, A., Sunderlikova, V., … Tans, S. J. (2022). Protein chain collapse modulation and folding stimulation by GroEL-ES. <i>Science Advances</i>. American Association for the Advancement of Science. <a href=\"https://doi.org/10.1126/sciadv.abl6293\">https://doi.org/10.1126/sciadv.abl6293</a>","ieee":"M. M. Naqvi <i>et al.</i>, “Protein chain collapse modulation and folding stimulation by GroEL-ES,” <i>Science Advances</i>, vol. 8, no. 9. American Association for the Advancement of Science, 2022.","chicago":"Naqvi, Mohsin M., Mario Avellaneda Sarrió, Andrew Roth, Eline J. Koers, Antoine Roland, Vanda Sunderlikova, Günter Kramer, Hays S. Rye, and Sander J. Tans. “Protein Chain Collapse Modulation and Folding Stimulation by GroEL-ES.” <i>Science Advances</i>. American Association for the Advancement of Science, 2022. <a href=\"https://doi.org/10.1126/sciadv.abl6293\">https://doi.org/10.1126/sciadv.abl6293</a>.","short":"M.M. Naqvi, M. Avellaneda Sarrió, A. Roth, E.J. Koers, A. Roland, V. Sunderlikova, G. Kramer, H.S. Rye, S.J. Tans, Science Advances 8 (2022).","mla":"Naqvi, Mohsin M., et al. “Protein Chain Collapse Modulation and Folding Stimulation by GroEL-ES.” <i>Science Advances</i>, vol. 8, no. 9, eabl6293, American Association for the Advancement of Science, 2022, doi:<a href=\"https://doi.org/10.1126/sciadv.abl6293\">10.1126/sciadv.abl6293</a>.","ista":"Naqvi MM, Avellaneda Sarrió M, Roth A, Koers EJ, Roland A, Sunderlikova V, Kramer G, Rye HS, Tans SJ. 2022. Protein chain collapse modulation and folding stimulation by GroEL-ES. Science Advances. 8(9), eabl6293."},"language":[{"iso":"eng"}],"acknowledgement":"We thank A. L. Horwich, K. Chakraborty, and B. Schuler for providing plasmids, and R. van Leeuwen, M. Mayer, J. van Zon, W. Noorduin, and P. R. ten Wolde for comments and critical reading of the manuscript. Work in the group of S.J.T. was supported by the Netherlands Organization for Scientific Research (NWO). Work in the group of H.S.R. was supported by a grant from the NIH (R01GM114405).","date_published":"2022-03-01T00:00:00Z","volume":8,"date_updated":"2024-07-31T12:03:54Z","oa":1,"type":"journal_article","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_number":"eabl6293","file":[{"file_name":"2022_ScienceAdv_Naqvi.pdf","content_type":"application/pdf","checksum":"9511579306cce7e04107d3d6389ed614","date_updated":"2024-07-31T12:01:51Z","creator":"dernst","access_level":"open_access","file_size":2404150,"success":1,"relation":"main_file","file_id":"17357","date_created":"2024-07-31T12:01:51Z"}],"publication_status":"published","publication_identifier":{"issn":["2375-2548"]},"department":[{"_id":"MiSi"}],"status":"public","doi":"10.1126/sciadv.abl6293","day":"01","has_accepted_license":"1","year":"2022","date_created":"2024-05-29T06:12:19Z","publication":"Science Advances","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","short":"CC BY (4.0)"},"file_date_updated":"2024-07-31T12:01:51Z","intvolume":"         8","month":"03"}