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Expression and preliminary characterization of human MICU2.
Li, Dan; Wu, Wenping; Pei, Hairun; Wei, Qiang; Yang, Qingzhan; Zheng, Jimin; Jia, Zongchao.
Afiliación
  • Li D; College of Chemistry, Beijing Normal University, Beijing 100875, China.
  • Wu W; College of Chemistry, Beijing Normal University, Beijing 100875, China.
  • Pei H; College of Chemistry, Beijing Normal University, Beijing 100875, China.
  • Wei Q; College of Chemistry, Beijing Normal University, Beijing 100875, China.
  • Yang Q; College of Chemistry, Beijing Normal University, Beijing 100875, China.
  • Zheng J; College of Chemistry, Beijing Normal University, Beijing 100875, China jimin_z@bnu.edu.cn jia@queensu.ca.
  • Jia Z; Department of Biochemical and Molecular Science, Queen University, Kingston, Ontario, Canada K7L 3N6 jimin_z@bnu.edu.cn jia@queensu.ca.
Biol Open ; 5(7): 962-9, 2016 Jul 15.
Article en En | MEDLINE | ID: mdl-27334695
MICU2 has been reported to interact with MICU1 and participate in the regulation of mitochondrial Ca(2+) uptake, although the molecular determinants underlying the function of MICU2 is unknown. In order to characterize MICU2 we screened a series of N-terminal and C-terminal truncations and obtained constructs which can be expressed in abundance, giving rise to soluble samples to enable subsequent characterizations. Size exclusion chromatography (SEC) and multi-angle laser light scattering (MALLS) revealed that MICU2 exists as a monomer in Ca(2+)-free conditions but forms a dimer in Ca(2+)-bound conditions. Unlike MICU1, the C-helix domain of MICU2 exhibits no influence on protein conformation in both Ca(2+)-free and Ca(2+)-bound forms. Furthermore, mutation of the first EF-hand abolishes the ability of MICU2 to switch to a dimer in the presence of Ca(2+), indicating that the first EF-hand is not only involved in Ca(2+) binding but also in conformational change. Our pull-down and co-immunoprecipitation assays suggest that, in addition to disulfide bonds, salt bridges also contribute to MICU1-MICU2 heterodimer formation.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Biol Open Año: 2016 Tipo del documento: Article País de afiliación: China Pais de publicación: Reino Unido
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Biol Open Año: 2016 Tipo del documento: Article País de afiliación: China Pais de publicación: Reino Unido