دورية أكاديمية

Mitochondrial F-ATP Synthase Co-Migrating Proteins and Ca 2+ -Dependent Formation of Large Channels.

التفاصيل البيبلوغرافية
العنوان: Mitochondrial F-ATP Synthase Co-Migrating Proteins and Ca 2+ -Dependent Formation of Large Channels.
المؤلفون: Nikiforova AB; Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Institutskaya 3, 142290 Pushchino, Russia., Baburina YL; Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Institutskaya 3, 142290 Pushchino, Russia., Borisova MP; Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Institutskaya 3, 142290 Pushchino, Russia., Surin AK; Branch of the Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Prospekt Nauki 6, 142290 Pushchino, Russia.; State Research Centre for Applied Microbiology and Biotechnology, 142279 Obolensk, Russia.; Institute of Protein Research, Russian Academy of Sciences, Institutskaya 4, 142290 Pushchino, Russia., Kharechkina ES; Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Institutskaya 3, 142290 Pushchino, Russia., Krestinina OV; Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Institutskaya 3, 142290 Pushchino, Russia., Suvorina MY; Institute of Protein Research, Russian Academy of Sciences, Institutskaya 4, 142290 Pushchino, Russia., Kruglova SA; Institute of Basic Biological Problems, Russian Academy of Sciences, Institutskaya 2, 142290 Pushchino, Russia., Kruglov AG; Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Institutskaya 3, 142290 Pushchino, Russia.
المصدر: Cells [Cells] 2023 Oct 07; Vol. 12 (19). Date of Electronic Publication: 2023 Oct 07.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: MDPI Country of Publication: Switzerland NLM ID: 101600052 Publication Model: Electronic Cited Medium: Internet ISSN: 2073-4409 (Electronic) Linking ISSN: 20734409 NLM ISO Abbreviation: Cells Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Basel, Switzerland : MDPI
مواضيع طبية MeSH: Mitochondrial Proton-Translocating ATPases*/metabolism , Mitochondrial Membrane Transport Proteins*/metabolism, Protein Subunits/metabolism ; Mitochondria, Heart/metabolism ; Adenosine Triphosphate
مستخلص: Monomers, dimers, and individual F O F 1 -ATP synthase subunits are, presumably, involved in the formation of the mitochondrial permeability transition pore (PTP), whose molecular structure, however, is still unknown. We hypothesized that, during the Ca 2+ -dependent assembly of a PTP complex, the F-ATP synthase (subunits) recruits mitochondrial proteins that do not interact or weakly interact with the F-ATP synthase under normal conditions. Therefore, we examined whether the PTP opening in mitochondria before the separation of supercomplexes via BN-PAGE will increase the channel stability and channel-forming capacity of isolated F-ATP synthase dimers and monomers in planar lipid membranes. Additionally, we studied the specific activity and the protein composition of F-ATP synthase dimers and monomers from rat liver and heart mitochondria before and after PTP opening. Against our expectations, preliminary PTP opening dramatically suppressed the high-conductance channel activity of F-ATP synthase dimers and monomers and decreased their specific "in-gel" activity. The decline in the channel-forming activity correlated with the reduced levels of as few as two proteins in the bands: methylmalonate-semialdehyde dehydrogenase and prohibitin 2. These results indicate that proteins co-migrating with the F-ATP synthase may be important players in PTP formation and stabilization.
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فهرسة مساهمة: Keywords: F-ATP synthase; dimer; high-conductance channel; methylmalonate–semialdehyde dehydrogenase; mitochondrial complex V; monomer; permeability transition pore; prohibitin
المشرفين على المادة: EC 3.6.3.- (Mitochondrial Proton-Translocating ATPases)
0 (Mitochondrial Membrane Transport Proteins)
0 (Protein Subunits)
8L70Q75FXE (Adenosine Triphosphate)
تواريخ الأحداث: Date Created: 20231013 Date Completed: 20231101 Latest Revision: 20231101
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC10572550
DOI: 10.3390/cells12192414
PMID: 37830628
قاعدة البيانات: MEDLINE
الوصف
تدمد:2073-4409
DOI:10.3390/cells12192414