دورية أكاديمية
أعرض في EDS

Unveiling the stochastic nature of human heteropolymer ferritin self-assembly mechanism.

التفاصيل البيبلوغرافية
العنوان: Unveiling the stochastic nature of human heteropolymer ferritin self-assembly mechanism.
المؤلفون: Bou-Abdallah F; Department of Chemistry, State University of New York, Potsdam, New York, USA., Fish J; Department of Electrical & Computer Engineering, Coulter School of Engineering, Clarkson University, Potsdam, New York, USA., Terashi G; Department of Biological Sciences and Department of Computer Science, Purdue University, West Lafayette, Indiana, USA., Zhang Y; Department of Biological Sciences and Department of Computer Science, Purdue University, West Lafayette, Indiana, USA., Kihara D; Department of Biological Sciences and Department of Computer Science, Purdue University, West Lafayette, Indiana, USA., Arosio P; Department of Molecular and Translational Medicine, University of Brescia, Brescia, Italy.
المصدر: Protein science : a publication of the Protein Society [Protein Sci] 2024 Aug; Vol. 33 (8), pp. e5104.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Cold Spring Harbor Laboratory Press Country of Publication: United States NLM ID: 9211750 Publication Model: Print Cited Medium: Internet ISSN: 1469-896X (Electronic) Linking ISSN: 09618368 NLM ISO Abbreviation: Protein Sci Subsets: MEDLINE
أسماء مطبوعة: Publication: 2001- : Woodbury, NY : Cold Spring Harbor Laboratory Press
Original Publication: New York, N.Y. : Cambridge University Press, c1992-
مواضيع طبية MeSH: Protein Multimerization* , Ferritins*/chemistry , Ferritins*/metabolism , Ferritins*/genetics, Humans ; Models, Molecular ; Cryoelectron Microscopy
مستخلص: Despite ferritin's critical role in regulating cellular and systemic iron levels, our understanding of the structure and assembly mechanism of isoferritins, discovered over eight decades ago, remains limited. Unveiling how the composition and molecular architecture of hetero-oligomeric ferritins confer distinct functionality to isoferritins is essential to understanding how the structural intricacies of H and L subunits influence their interactions with cellular machinery. In this study, ferritin heteropolymers with specific H to L subunit ratios were synthesized using a uniquely engineered plasmid design, followed by high-resolution cryo-electron microscopy analysis and deep learning-based amino acid modeling. Our structural examination revealed unique architectural features during the self-assembly mechanism of heteropolymer ferritins and demonstrated a significant preference for H-L heterodimer formation over H-H or L-L homodimers. Unexpectedly, while dimers seem essential building blocks in the protein self-assembly process, the overall mechanism of ferritin self-assembly is observed to proceed randomly through diverse pathways. The physiological significance of these findings is discussed including how ferritin microheterogeneity could represent a tissue-specific adaptation process that imparts distinctive tissue-specific functions to isoferritins.
(© 2024 The Protein Society.)
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معلومات مُعتمدة: 1934666 National Science Foundation, Division of Molecular and Cellular Biosciences (MCB); R01GM133840 United States NH NIH HHS; DBI2003635 National Science Foundation; DBI2146026 National Science Foundation; IIS2211598 National Science Foundation; DMS2151678 National Science Foundation; CMMI1825941 National Science Foundation; 27452 Research Corporation for Science Advancement, Cottrell Instrumentation Supplements Award
فهرسة مساهمة: Keywords: cryo‐EM; ferritin microheterogeneity; ferritin subunits; human heteropolymer ferritin; isoferritins; self‐assembly mechanism
المشرفين على المادة: 9007-73-2 (Ferritins)
تواريخ الأحداث: Date Created: 20240712 Date Completed: 20240712 Latest Revision: 20240714
رمز التحديث: 20240714
مُعرف محوري في PubMed: PMC11241160
DOI: 10.1002/pro.5104
PMID: 38995055
قاعدة البيانات: MEDLINE
الوصف
تدمد:1469-896X
DOI:10.1002/pro.5104