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Characterization of the interaction between superoxide dismutase and 2-oxoisovalerate dehydrogenase.

التفاصيل البيبلوغرافية
العنوان: Characterization of the interaction between superoxide dismutase and 2-oxoisovalerate dehydrogenase.
المؤلفون: Song C; Key Laboratory of Conservation Biology for Endangered Wildlife of Ministry of Education and College of Life Sciences, Zhejiang University, Hangzhou 310058, People's Republic of China; School of Chemistry and Material Engineering, Fuyang Teachers College, Fuyang 236037, People's Republic of China., Li H; Key Laboratory of Marine Biogenetic Resources, Third Institute of Oceanography, State Oceanic Administration, Xiamen 361005, People's Republic of China., Sheng L; School of Chemistry and Material Engineering, Fuyang Teachers College, Fuyang 236037, People's Republic of China., Zhang X; Key Laboratory of Conservation Biology for Endangered Wildlife of Ministry of Education and College of Life Sciences, Zhejiang University, Hangzhou 310058, People's Republic of China. Electronic address: zxb0812@zju.edu.cn.
المصدر: Gene [Gene] 2015 Aug 15; Vol. 568 (1), pp. 1-7. Date of Electronic Publication: 2015 May 07.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Elsevier/North-Holland Country of Publication: Netherlands NLM ID: 7706761 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-0038 (Electronic) Linking ISSN: 03781119 NLM ISO Abbreviation: Gene Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Amsterdam, Elsevier/North-Holland, 1976-
مواضيع طبية MeSH: 2-Oxoisovalerate Dehydrogenase (Acylating)/*metabolism , Bacterial Proteins/*metabolism , Superoxide Dismutase/*metabolism , Thermus thermophilus/*enzymology, 2-Oxoisovalerate Dehydrogenase (Acylating)/chemistry ; Adaptation, Physiological ; Amino Acid Sequence ; Bacterial Proteins/chemistry ; Molecular Sequence Data ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein Interaction Mapping ; Superoxide Dismutase/chemistry ; Thermodynamics
مستخلص: Thermophiles are attractive microorganisms to study the adaptation of life in high temperature environment. It is revealed that superoxide dismutase (SOD) is essential for thermoadaptation of thermophiles. However, the SOD-mediated pathway of thermoadaptation remains unclear. To address this issue, the proteins interacted with SOD were characterized in Thermus thermophilus in this study. Based on co-immunoprecipitation and Western blot analyses, the results showed that 2-oxoisovalerate dehydrogenase α subunit was bound to SOD. The isothermal titration calorimetry analysis showed the existence of the interaction between SOD and 2-oxoisovalerate dehydrogenase α subunit. The bacterial two-hybrid data indicated that SOD was directly interacted with 2-oxoisovalerate dehydrogenase α subunit. Gene site-directed mutagenesis analysis revealed that the intracellular interaction between SOD and 2-oxoisovalerate dehydrogenase α subunit was dependent on their whole molecules. Therefore our study presented a novel aspect of SOD in the thermoadaptation of thermophiles by interaction with dehydrogenase, a key enzyme of tricarboxylic acid cycle.
(Copyright © 2015 Elsevier B.V. All rights reserved.)
فهرسة مساهمة: Keywords: 2-Oxoisovalerate dehydrogenase α subunit; Protein interaction; Superoxide dismutase; Thermoadaptation; Thermus thermophilus
المشرفين على المادة: 0 (Bacterial Proteins)
EC 1.15.1.1 (Superoxide Dismutase)
EC 1.2.1.25 (2-Oxoisovalerate Dehydrogenase (Acylating))
تواريخ الأحداث: Date Created: 20150511 Date Completed: 20150819 Latest Revision: 20150616
رمز التحديث: 20240628
DOI: 10.1016/j.gene.2015.05.008
PMID: 25958347
قاعدة البيانات: MEDLINE
الوصف
تدمد:1879-0038
DOI:10.1016/j.gene.2015.05.008