دورية أكاديمية
أعرض في EDS

The cofactor-dependent folding mechanism of Drosophila cryptochrome revealed by single-molecule pulling experiments.

التفاصيل البيبلوغرافية
العنوان: The cofactor-dependent folding mechanism of Drosophila cryptochrome revealed by single-molecule pulling experiments.
المؤلفون: Foroutannejad S; Department of Chemistry, Georgetown University, Washington, DC, USA., Good LL; Department of Chemistry, Georgetown University, Washington, DC, USA., Lin C; Department of Chemistry & Chemical Biology, Cornell University, Ithaca, NY, USA., Carter ZI; Department of Chemistry, University of Alabama at Birmingham, Birmingham, AL, USA., Tadesse MG; Department of Mathematics and Statistics, Georgetown University, Washington, DC, USA., Lucius AL; Department of Chemistry, University of Alabama at Birmingham, Birmingham, AL, USA., Crane BR; Department of Chemistry & Chemical Biology, Cornell University, Ithaca, NY, USA., Maillard RA; Department of Chemistry, Georgetown University, Washington, DC, USA. rodrigo.maillard@georgetown.edu.
المصدر: Nature communications [Nat Commun] 2023 Feb 24; Vol. 14 (1), pp. 1057. Date of Electronic Publication: 2023 Feb 24.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
اللغة: English
بيانات الدورية: Publisher: Nature Pub. Group Country of Publication: England NLM ID: 101528555 Publication Model: Electronic Cited Medium: Internet ISSN: 2041-1723 (Electronic) Linking ISSN: 20411723 NLM ISO Abbreviation: Nat Commun Subsets: MEDLINE
أسماء مطبوعة: Original Publication: [London] : Nature Pub. Group
مواضيع طبية MeSH: Drosophila*/metabolism , Cryptochromes*/metabolism, Animals ; Proteins/metabolism ; Protein Folding ; Flavin-Adenine Dinucleotide/metabolism
مستخلص: The link between cofactor binding and protein activity is well-established. However, how cofactor interactions modulate folding of large proteins remains unknown. We use optical tweezers, clustering and global fitting to dissect the folding mechanism of Drosophila cryptochrome (dCRY), a 542-residue protein that binds FAD, one of the most chemically and structurally complex cofactors in nature. We show that the first dCRY parts to fold are independent of FAD, but later steps are FAD-driven as the remaining polypeptide folds around the cofactor. FAD binds to largely unfolded intermediates, yet with association kinetics above the diffusion-limit. Interestingly, not all FAD moieties are required for folding: whereas the isoalloxazine ring linked to ribitol and one phosphate is sufficient to drive complete folding, the adenosine ring with phosphates only leads to partial folding. Lastly, we propose a dCRY folding model where regions that undergo conformational transitions during signal transduction are the last to fold.
(© 2023. The Author(s).)
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معلومات مُعتمدة: R35 GM122535 United States GM NIGMS NIH HHS; R15 GM135866 United States GM NIGMS NIH HHS
المشرفين على المادة: 0 (Cryptochromes)
0 (Proteins)
146-14-5 (Flavin-Adenine Dinucleotide)
تواريخ الأحداث: Date Created: 20230224 Date Completed: 20230228 Latest Revision: 20231117
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC9958137
DOI: 10.1038/s41467-023-36701-y
PMID: 36828841
قاعدة البيانات: MEDLINE
الوصف
تدمد:2041-1723
DOI:10.1038/s41467-023-36701-y