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Opposite roles of group IV BBX proteins: Exploring missing links between structural and functional diversity

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dc.contributor.author Yadukrishnan, Premachandran
dc.date.accessioned 2026-01-06T11:29:34Z
dc.date.available 2026-01-06T11:29:34Z
dc.date.issued 2018-08
dc.identifier.uri https://www.tandfonline.com/doi/full/10.1080/15592324.2018.1462641
dc.identifier.uri http://dspace.bits-pilani.ac.in:8080/jspui/handle/123456789/20499
dc.description.abstract BBX proteins are a family of zinc finger transcription factors that are versatile regulators of plant development. The 32 BBX proteins in Arabidopsis are subdivided into five structural groups based on their domain structure. Members of group IV play important and diverse roles in light-regulated development. The N-terminal B-box domains mediate DNA binding and transcriptional regulation. The C-terminal region determines the functional diversity of the structurally similar group IV members as reported in our recent study investigating the basis of functional diversification between BBX21 and BBX24. We also found that multi-layered regulation of HY5 by the BBX proteins leads to a diverse repertoire of developmental effects. Here we provide a comprehensive structure-function analysis of the group IV BBX proteins. en_US
dc.language.iso en en_US
dc.publisher Taylor & Francis en_US
dc.subject Biology en_US
dc.subject B-box en_US
dc.subject BBX21 en_US
dc.subject BBX24 en_US
dc.subject HY5 en_US
dc.subject Light signaling en_US
dc.subject Photomorphogenesis en_US
dc.title Opposite roles of group IV BBX proteins: Exploring missing links between structural and functional diversity en_US
dc.type Article en_US


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