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Ca2+ -Calmodulin regulates nuclear translocation of the rice seed-specific MADS-box transcription factor OsMADS29.
Verma, Vibha; Boora, Neelima; Nayar, Saraswati; Kumar, Gulshan; Thapliyal, Somesh; Khurana, Ridhi; Gawande, Gautam; Kapoor, Meenu; Kapoor, Sanjay.
Afiliación
  • Verma V; Interdisciplinary Centre for Plant Genomics, Department of Plant Molecular Biology, University of Delhi South Campus, India.
  • Boora N; Interdisciplinary Centre for Plant Genomics, Department of Plant Molecular Biology, University of Delhi South Campus, India.
  • Nayar S; Interdisciplinary Centre for Plant Genomics, Department of Plant Molecular Biology, University of Delhi South Campus, India.
  • Kumar G; Interdisciplinary Centre for Plant Genomics, Department of Plant Molecular Biology, University of Delhi South Campus, India.
  • Thapliyal S; Interdisciplinary Centre for Plant Genomics, Department of Plant Molecular Biology, University of Delhi South Campus, India.
  • Ankur; Interdisciplinary Centre for Plant Genomics, Department of Plant Molecular Biology, University of Delhi South Campus, India.
  • Khurana R; Interdisciplinary Centre for Plant Genomics, Department of Plant Molecular Biology, University of Delhi South Campus, India.
  • Gawande G; Interdisciplinary Centre for Plant Genomics, Department of Plant Molecular Biology, University of Delhi South Campus, India.
  • Kapoor M; University School of Biotechnology, Guru Gobind Singh Indraprastha University, Dwarka, New Delhi, India.
  • Kapoor S; Interdisciplinary Centre for Plant Genomics, Department of Plant Molecular Biology, University of Delhi South Campus, India.
FEBS J ; 290(14): 3595-3613, 2023 07.
Article en En | MEDLINE | ID: mdl-36861329
OsMADS29 (M29) is a crucial regulator of seed development in rice. The expression of M29 is strictly regulated at transcriptional as well as post-transcriptional levels. The MADS-box proteins are known to bind to DNA as dimers. However, in the case of M29, the dimerization also plays a vital role in its localization into the nucleus. The factor(s) that affect oligomerization and nuclear transport of MADS proteins have not yet been characterized. By using BiFC in transgenic BY-2 cell lines and Yeast-2-hybrid assay (Y2H), we show that calmodulin (CaM) interacts with M29 in a Ca2+ -dependent manner. This interaction specifically takes place in the cytoplasm, probably in association with the endoplasmic reticulum. By generating domain-specific deletions, we show that both sites in M29 are involved in this interaction. Further, by using BiFC-FRET-FLIM, we demonstrate that CaM may also help in the dimerization of two M29 monomers. Since most MADS proteins have CaM binding domains, the interaction between these proteins could be a general regulatory mechanism for oligomerization and nuclear transport.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Oryza / Factores de Transcripción Idioma: En Revista: FEBS J Asunto de la revista: BIOQUIMICA Año: 2023 Tipo del documento: Article País de afiliación: India Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Oryza / Factores de Transcripción Idioma: En Revista: FEBS J Asunto de la revista: BIOQUIMICA Año: 2023 Tipo del documento: Article País de afiliación: India Pais de publicación: Reino Unido