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Molecular organizations and function of iron-stress-induced-A protein family in Anabaena sp. PCC 7120.
Nagao, Ryo; Yokono, Makio; Ueno, Yoshifumi; Suzuki, Takehiro; Kato, Koji; Kato, Ka-Ho; Tsuboshita, Naoki; Jiang, Tian-Yi; Dohmae, Naoshi; Shen, Jian-Ren; Ehira, Shigeki; Akimoto, Seiji.
Afiliación
  • Nagao R; Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama 700-8530, Japan. Electronic address: nagaoryo@okayama-u.ac.jp.
  • Yokono M; Institute of Low Temperature Science, Hokkaido University, Hokkaido 060-0819, Japan.
  • Ueno Y; Graduate School of Science, Kobe University, Hyogo 657-8501, Japan.
  • Suzuki T; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Saitama 351-0198, Japan.
  • Kato K; Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama 700-8530, Japan.
  • Kato KH; Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama 700-8530, Japan.
  • Tsuboshita N; Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama 700-8530, Japan.
  • Jiang TY; Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama 700-8530, Japan.
  • Dohmae N; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Saitama 351-0198, Japan.
  • Shen JR; Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama 700-8530, Japan.
  • Ehira S; Department of Biological Sciences, Graduate School of Science, Tokyo Metropolitan University, Tokyo 192-0397, Japan. Electronic address: ehira@tmu.ac.jp.
  • Akimoto S; Graduate School of Science, Kobe University, Hyogo 657-8501, Japan. Electronic address: akimoto@hawk.kobe-u.ac.jp.
Biochim Biophys Acta Bioenerg ; 1862(1): 148327, 2021 01 01.
Article en En | MEDLINE | ID: mdl-33069682
Iron-stress-induced-A proteins (IsiAs) are expressed in cyanobacteria under iron-deficient conditions, and surround photosystem I (PSI) trimer with a ring formation. A cyanobacterium Anabaena sp. PCC 7120 has four isiA genes; however, it is unknown how the IsiAs are associated with PSI. Here we report on molecular organizations and function of the IsiAs in this cyanobacterium. A deletion mutant of the isiA1 gene was constructed, and the four types of thylakoids were prepared from the wild-type (WT) and ΔisiA1 cells under iron-replete (+Fe) and iron-deficient (-Fe) conditions. Immunoblotting analysis exhibits a clear expression of the IsiA1 in the WT-Fe. The PSI-IsiA1 supercomplex is found in the WT-Fe, and excitation-energy transfer from IsiA1 to PSI is verified by time-resolved fluorescence analyses. Instead of the IsiA1, both IsiA2 and IsiA3 are bound to PSI monomer in the ΔisiA1-Fe. These findings provide insights into multiple-expression system of the IsiA family in this cyanobacterium.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Familia de Multigenes / Anabaena / Complejos de Proteína Captadores de Luz / Hierro Idioma: En Revista: Biochim Biophys Acta Bioenerg Año: 2021 Tipo del documento: Article

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Familia de Multigenes / Anabaena / Complejos de Proteína Captadores de Luz / Hierro Idioma: En Revista: Biochim Biophys Acta Bioenerg Año: 2021 Tipo del documento: Article