1998
DOI: 10.1016/s0014-5793(98)00670-x
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Functional analyses of the Dof domain, a zinc finger DNA‐binding domain, in a pumpkin DNA‐binding protein AOBP

Abstract: AOBP, a DNA-binding protein in pumpkin, contains a Dof domain that is composed of 52 amino acid residues and is highly conserved in several DNA-binding proteins of higher plants. The Dof domain has a significant resemblance to Cys2/ Cys2 zinc finger DNA-binding domains of steroid hormone receptors and GATA1, but has a longer putative loop where an extra Cys residue is conserved. We show that the Dof domain in AOBP functions as a zinc finger DNA-binding domain and suggest that the Cys residue uniquely conserved… Show more

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Cited by 42 publications
(29 citation statements)
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“…AOBP encodes a Dof/Zn-finger transcription factor that is proposed to repress AOX transcription and cause the accumulation of reduced ASC Shimofurutani et al, 1998). In contrast with these reports, our transcriptome and selective metabolite analyses show that AOBP expression is not positively correlated with ASC accumulation in tomato pericarp (Figure 4; see Supplemental Figure 1 online) and therefore imply that this metabolite is governed by factors in addition to or other than AOBP in this tissue.…”
Section: Candidate Regulatory Genes For Fruit Developmentcontrasting
confidence: 97%
“…AOBP encodes a Dof/Zn-finger transcription factor that is proposed to repress AOX transcription and cause the accumulation of reduced ASC Shimofurutani et al, 1998). In contrast with these reports, our transcriptome and selective metabolite analyses show that AOBP expression is not positively correlated with ASC accumulation in tomato pericarp (Figure 4; see Supplemental Figure 1 online) and therefore imply that this metabolite is governed by factors in addition to or other than AOBP in this tissue.…”
Section: Candidate Regulatory Genes For Fruit Developmentcontrasting
confidence: 97%
“…For example, OsMADS45 interacted with an undefined protein whose gene expression is induced in seeds. This undefined protein interacted with two ZFPs with a defined promoter-binding element (35) and with DOF domains resembling the Cys-2͞Cys-2 zinc finger DNAbinding domains of steroid receptors (36). The first DOF ZFP interacted with a protein with a basic helix-loop-helix domain shared across kingdoms by a class of TFs responsible for developmental transcription (37), supporting the notion of an extended TF interaction network for developmental control.…”
Section: Resultsmentioning
confidence: 68%
“…When Cys 65 was replaced by Ala, the protein lost its capacity to bind Pb3 and also transactivate cZ. This indicates that the Cys2/ Cys2 Zn 2+ structure is necessary to maintain the proper conformation for DNA binding, as it has been previously described for other Dof transcription factors (Mena et al 1998;Shimofurutani et al 1998;Yanagisawa 1995). In addition to Cys residues, it appears that aromatic residues (Y and W) in the C-terminal part of Dof domain contribute to stabilize the Dof structure (Umemura et al 2004).…”
Section: Functional Domains Of Pbfmentioning
confidence: 65%