Abstract
A 5′ flaking nucleotide sequence of 1,101 bp of rice catalase-B gene (CatB) coding sequence having coordinates from −808 to +294 with respect to the transcription start site was transcriptionally fused to the β-glucuronidase gene (GUS), and functionally analyzed through transient and stable expression assay systems to identify the minimal promoter sequence containing the important cis-regulatory regions controlling its expression. The progressive up-stream and down-stream (5′/3′) deletion analysis of the 1,101-bp fragment revealed that minimal nucleotide sequences spanning from −121 to +56 possessed maximum GUS activity, which was nearly six- to eightfold higher than GUS activity driven by CaMV35S promoter. DNase I footprint and gel retardation analysis of the minimal promoter sequence with nuclear extract revealed the presence of a “AAAAG” nucleotide signature referring to DNA-binding with one finger (Dof) transcription factor. In addition, the presence of CAAT-box sequence was also evident. The Dof interacting sequence in CatB promoter of rice has been established for the first time in this work.
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Bhattacharya S, Dey N, Maiti IB. Analysis of cis-sequence of sub-genomic transcript promoter from the Figwort mosaic virus and comparison of promoter activity with the Cauliflower mosaic virus promoters in monocot and dicot cells. Virus Res 2002;90:47–62.
Bradford MM. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of dye binding. Anal Biochem 1976;72:248–54.
Dey N, Maiti IB. Structure and promoter/leader deletion analysis of mirabilis mosaic virus (MMV) full-length transcript promoter in transgenic plants. Plant Mol Biol 1999a;40:771–82.
Dey N, Maiti IB. Characterization and expression analysis of Mirabilis Mosaic Caulimovirus (MMV) Full-length transcript promoter with single and double enhancer domains in transgenic plants. Transgenics 1999b;3:61–70.
Feierabend J. Catalase in plants: molecular and functional properties and role in stress defence. In: Smirnoff N, editor. Antioxidant and reactive oxygen species in plants. Oxford: Blackwell; 2005. p. 101–40.
Fromm M, Callis J, Taylor LP, Walbo V. Electroporation of DNA and RNA into plant protoplasts. Methods Enzymol 1987;153:351–66.
Guan LM, Zhao J, Scandalios JG. Cis-element and trans-factors that regulate expression of the maize Cat1 antioxidant gene in response to ABA and osmotic stress: H2O2 is the likely intermediary signaling molecule for the response. Plant J 2000;22:87–95.
Hettiarachchi GHCM, Reddy MK, Sopory SK, Chattopadhyay S. Regulation of TOP 2 by various abiotic stresses including cold and salinity in pea and transgenic tobacco plants. Plant Cell Physiol 2005;46:1154–60.
Higo K, Ugawa Y, Iwamoto M, Korenaga T. Plant cis-acting regulatory DNA elements (PLACE) database. Nucleic Acids Res 1999;27:297–300.
Iwamoto M, Higo H, Higo K. Differential diurnal expression of rice catalase genes; the 5’ flanking region of CatA is not sufficient for circadian control. Plant Sci 2000;151:39–46.
Iwamoto M, Higo H, Higo K. Strong expression of the rice catalase gene CatB promoter in protoplast and roots of both a monocot and dicot. Plant Physiol Biochem 2004;42:241–9.
Jefferson RA, Kavanagh TA, Bevan MW. GUS fusion β-glucuronidase as a sensitive and versatile gene fusion marker in higher plants. EMBO J 1987;6:3901–7.
Lodhi MA, Ye GN, Weeden NF, Reisch BI. A simple and efficient method for DNA extraction from grapevine cultivars and vitis species. Plant Mol Biol Rep 1994;12:6–13.
Maiti IB, Murphy JF, Shaw JG, Hunt AG. Plant that express a poly virus proteinase gene are resistant to virus infection. Proc Natl Acad Sci USA 1993;90:6110–4.
Sambrook J, Fritsch EF, Maniatis T. Molecular cloning; a laboratory manual. Cold spring Harbor: Cold Spring Harbor Laboratory Press; 1989.
Sangar F, Nicklen S, Coulson AR. DNA sequencing with chain termination inhibitor. Proc Natl Acad Sci USA 1977;74:5463–7.
Vetrano MA, Heck ED, Mariano MT, Mishin V, Laskin LD, Laskin DJ. Characterization of oxidase activity in mammalian catalase. J Biol Chem 2005;280:35372–81.
Willekens HD, Inze D, Van Montagu M, van Camp W. Catalase in plants. Mol Breed 1995;1:207–28.
Yanagisawa S. Dof domain proteins: Plant-specific transcription factors associated with diverse phenomena unique to plants. Plant Cell Physiol 2004;45:386–91.
Zaret KS, Liu J-K, Dipersio CM. Site-directed mutagenesis reveals a liver transcription factor essential for albumin transcriptional enhances. Proc Natl Acad Sci USA 1990;87:5469–73.
Acknowledgements
The financial support from the Department of Biotechnology, Government of India, to PM in the form of a senior research fellowship in full and to AKD in part are gratefully acknowledged. The authors are thankful to the Director of the Institute of Life Sciences, Bhubaneswar, for his interest in this research and support.
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Mondal, P., Dey, N., Dash, A.K. et al. Structural and Functional Analysis of Rice Catalase-B Gene Promoter: Presence of Dof and CAAT Binding Site. Plant Mol Biol Rep 25, 71–82 (2007). https://doi.org/10.1007/s11105-007-0011-6
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DOI: https://doi.org/10.1007/s11105-007-0011-6