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Please use this identifier to cite or link to this item: http://dspace.bits-pilani.ac.in:8080/jspui/handle/123456789/20499
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dc.contributor.authorYadukrishnan, Premachandran-
dc.date.accessioned2026-01-06T11:29:34Z-
dc.date.available2026-01-06T11:29:34Z-
dc.date.issued2018-08-
dc.identifier.urihttps://www.tandfonline.com/doi/full/10.1080/15592324.2018.1462641-
dc.identifier.urihttp://dspace.bits-pilani.ac.in:8080/jspui/handle/123456789/20499-
dc.description.abstractBBX 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.isoenen_US
dc.publisherTaylor & Francisen_US
dc.subjectBiologyen_US
dc.subjectB-boxen_US
dc.subjectBBX21en_US
dc.subjectBBX24en_US
dc.subjectHY5en_US
dc.subjectLight signalingen_US
dc.subjectPhotomorphogenesisen_US
dc.titleOpposite roles of group IV BBX proteins: Exploring missing links between structural and functional diversityen_US
dc.typeArticleen_US
Appears in Collections:Department of Biological Sciences

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