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. 2023 Jul;290(14):3595-3613.
doi: 10.1111/febs.16767. Epub 2023 Mar 20.

Ca2+ -Calmodulin regulates nuclear translocation of the rice seed-specific MADS-box transcription factor OsMADS29

Vibha Verma  1 , Neelima Boora  1 , Saraswati Nayar  1 , Gulshan Kumar  1 , Somesh Thapliyal  1 , Ankur  1 , Ridhi Khurana  1 , Gautam Gawande  1 , Meenu Kapoor  2 , Sanjay Kapoor  1
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Free article

Ca2+ -Calmodulin regulates nuclear translocation of the rice seed-specific MADS-box transcription factor OsMADS29

Vibha Verma et al. FEBS J. 2023 Jul.
Free article

Abstract

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.

Keywords: MADS-box; calcium; calmodulin; cytoplasmic retention; nuclear transport; seed development.

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