دورية أكاديمية
Unfolding of bZIP dimers formed by the ATF-2 and c-Jun transcription factors is not a simple two-state transition.
| العنوان: | Unfolding of bZIP dimers formed by the ATF-2 and c-Jun transcription factors is not a simple two-state transition. |
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| المؤلفون: | Carrillo RJ; Department of Biology, Johns Hopkins University, Baltimore, MD 21218-2685, United States., Privalov PL |
| المصدر: | Biophysical chemistry [Biophys Chem] 2010 Oct; Vol. 151 (3), pp. 149-54. Date of Electronic Publication: 2010 Jun 23. |
| نوع المنشور: | Journal Article; Research Support, N.I.H., Extramural |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Science B.V Country of Publication: Netherlands NLM ID: 0403171 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1873-4200 (Electronic) Linking ISSN: 03014622 NLM ISO Abbreviation: Biophys Chem Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Amsterdam : Elsevier Science B.V Original Publication: Amsterdam, North-Holland Pub. Co. |
| مواضيع طبية MeSH: | Protein Multimerization* , Protein Unfolding*, Activating Transcription Factor 2/*chemistry , Activating Transcription Factor 2/*metabolism , Proto-Oncogene Proteins c-jun/*chemistry , Proto-Oncogene Proteins c-jun/*metabolism, Amino Acid Sequence ; Calorimetry ; Fluorescence Polarization ; Humans ; Molecular Sequence Data ; Protein Structure, Quaternary ; Temperature |
| مستخلص: | The varied selectivity of bZIP transcription factors stems from the fact that they are dimers consisting of two not necessarily identical subunits held together by a leucine zipper dimerization domain. Determining their stability is therefore important for understanding the mechanism of formation of these transcription factors. The most widely used approach for this problem consists of observing temperature-induced dissociation of the bZIPs by any means sensitive to their structural changes, particularly optical methods. In calculating thermodynamic characteristics of this process from such data it is usually assumed that it represents a two-state transition. However, scanning micro-calorimetric study of the temperature-induced unfolding/dissociation of the three bZIPs formed by the ATF-2 and c-Jun proteins, i.e. the two homodimers (ATF-2/ATF-2) and (c-Jun/c-Jun) and the heterodimer (ATF-2/c-Jun), showed that this process does not represent a two-state transition, as found previously with the GCN4 homodimeric bZIP protein. This raises doubt about all indirect estimates of bZIP thermodynamic characteristics based on analysis of their optically-observed temperature-induced changes. (2010 Elsevier B.V. All rights reserved.) |
| معلومات مُعتمدة: | R01 A1080828 United States PHS HHS |
| المشرفين على المادة: | 0 (Activating Transcription Factor 2) 0 (Proto-Oncogene Proteins c-jun) |
| تواريخ الأحداث: | Date Created: 20100713 Date Completed: 20101130 Latest Revision: 20100823 |
| رمز التحديث: | 20240829 |
| DOI: | 10.1016/j.bpc.2010.06.004 |
| PMID: | 20619956 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1873-4200 |
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| DOI: | 10.1016/j.bpc.2010.06.004 |