Please use this identifier to cite or link to this item: http://223.31.159.10:8080/jspui/handle/123456789/388
Title: Arabidopsis CAM7 and HY5 physically interact and directly bind to the HY5 promoter to regulate its expression and thereby promote photomorphogenesis
Authors: Abbas, Nazia
Maurya, Jay P.
Senapati, Dhirodatta
Gangappa, Sreeramaiah N.
Chattopadhyay, Sudip
Keywords: Arabidopsis thaliana
CALMODULIN7
HYPOCOTYL5
Photomorphogenesis
Issue Date: 2014
Publisher: American Society of Plant Biologists
Citation: Plant Cell, 26(3): 1036-1052
Abstract: Arabidopsis thaliana CALMODULIN7 (CAM7), a unique member of the calmodulin gene family, plays a crucial role as a transcriptional regulator in seedling development. The elongated HYPOCOTYL5 (HY5) bZIP protein, an integrator of multiple signaling pathways, also plays an important role in photomorphogenic growth and light-regulated gene expression. CAM7 acts synergistically with HY5 to promote photomorphogenesis at various wavelengths of light. Although the genetic relationships between CAM7 and HY5 in light-mediated seedling development have been demonstrated, the molecular connectivity between CAM7 and HY5 is unknown. Furthermore, whereas HY5-mediated gene regulation has been fairly well investigated, the transcriptional regulation of HY5 is largely unknown. Here, we report that HY5 expression is regulated by HY5 and CAM7 at various wavelengths of light and also at various stages of development. In vitro and in vivo DNA-protein interaction studies suggest that HY5 and CAM7 bind to closely located T/G- and E-box cis-acting elements present in the HY5 promoter, respectively. Furthermore, CAM7 and HY5 physically interact and regulate the expression of HY5 in a concerted manner. Taken together, these results demonstrate that CAM7 and HY5 directly interact with the HY5 promoter to mediate the transcriptional activity of HY5 during Arabidopsis seedling development.
Description: Accepted date: February 12, 2014
URI: http://172.16.0.77:8080/jspui/handle/123456789/388
ISSN: 1532-298X
Appears in Collections:Institutional Publications

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