若林 憲一
   所属   京都産業大学  生命科学部 産業生命科学科
   職種   教授
言語種別 英語
発行・発表の年月 2020/11
形態種別 研究論文
査読 査読あり
標題 Chloroplast ATP synthase is reduced by both f-type and m-type thioredoxins
執筆形態 その他
掲載誌名 Biochimica et Biophysica Acta (BBA) - Bioenergetics
掲載区分国外
出版社・発行元 Elsevier BV
巻・号・頁 1861(11),pp.148261-148261
著者・共著者 Takatoshi Sekiguchi,Keisuke Yoshida,Yuki Okegawa,Ken Motohashi,Ken-ichi Wakabayashi,Toru Hisabori
概要 The activity of the molecular motor enzyme, chloroplast ATP synthase, is regulated in a redox-dependent manner. The γ subunit, CF1-γ, is the central shaft of this enzyme complex and possesses the redox-active cysteine pair, which is reduced by thioredoxin (Trx). In light conditions, Trx transfers the reducing equivalent obtained from the photosynthetic electron transfer system to the CF1-γ. Previous studies showed that the light-dependent reduction of CF1-γ is more rapid than those of other Trx target proteins in the stroma. Although there are multiple Trx isoforms in chloroplasts, it is not well understood as to which chloroplast Trx isoform primarily contributes to the reduction of CF1-γ, especially under physiological conditions. We therefore performed direct assessment of the CF1-γ reduction capacity of each of the Trx isoforms. The kinetic analysis of the reduction process showed no significant difference in the reduction efficiency between two major chloroplast Trxs, namely Trx-f and Trx-m. Based on the thorough analyses of the CF1-γ redox dynamics in Arabidopsis thaliana Trx mutant plants, we found that lack of Trx-f or Trx-m had no significant impact on the in vivo light-dependent reduction of CF1-γ. The results showed that CF1-γ can accept the reducing power from both Trx-f and Trx-m in chloroplasts.
DOI 10.1016/j.bbabio.2020.148261
ISSN 0005-2728
PMID 32659266
Put Code(ORCID) 97421858