In vivo and in vitro characterization of protein interactions with the dyad G-box of the Arabidopsis Adh gene.

McKendree, William L.; Paul, Anna‐Lisa; DeLisle, Alice J.; Ferl, Robert J.

doi:10.1105/tpc.2.3.207

Cited by 69 publications

(56 citation statements)

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“…Leu zipper (b-Z1P)-type transcription factors interact with the G-box (Schindler et al, 1992b. Gel retardation and protein purification studies have shown that the Arabidopsis Adh G-box-1 sequence interacts with a nuclear protein McKendree et al, 1990).…”

Section: Dlscusslonmentioning

confidence: 99%

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Differential Interactions of Promoter Elements in Stress Responses of the Arabidopsis Adh Gene

et al. 1994

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The Adh (alcohol dehydrogenase, EC 1.1.1.1.) gene from Arabidopsis thaliana (1.) Heynh. can be induced by dehydration and cold, as well as by hypoxia. A 1-kb promoter fragment (CADH: -964 to +53) is sufficient to confer the stress indudion and tissuespecific developmental expression characteristics of the Adh gene to a 8-glucuronidase reporter gene. Deletion mapping of the 5' end and site-specific mutagenesis identified four regions of the promoter essential for expression under the three stress conditions. Some sequence elements are important for response to all three stress treatments, whereas others are stress specific. The most critical region essential for expression of the Arabidopsis Adh promoter under all three environmental stresses (region I V -172 to -141) contains sequences homologous to the CT motif (-160 to -152)

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Section: Dlscusslonmentioning

confidence: 99%

“…Vol. 105,1994 with a GBF (Schindler et al, 1992d), and it was shown that a GBF does interact with this G-box McKendree et al, 1990). We will refer to this sequence as the G-box-1 sequence.…”

Section: The Regions Of the Arabidopsis A D H Promoter Responsiblementioning

confidence: 99%

Differential Interactions of Promoter Elements in Stress Responses of the Arabidopsis Adh Gene

et al. 1994

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“…Whole cell protein extracts (13) were made from the cell suspensions by the methods of McKendree et al (14). The final dialysis buffer was NEBD with 40 mM KCI.…”

Section: Whole Cell Extracts and Fractionationsmentioning

confidence: 99%

ARF-B₂: A Protein Complex that Specifically Binds to Part of the Anaerobic Response Element of Maize Adh 1

Ferl¹

1990

Plant Physiol.

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Crude whole cell extracts from maize (Zea mays L.) suspension cells were examined for DNA binding proteins that specifically interact with a portion of the maize Adhl promoter that was previously shown to be in contact with a trans-acting factor in vivo. A 17 base pair, double-stranded oligonucleotide probe was constructed that centered around a strong in vivo dimethylsulfate footprint (B2) that coincides with part of the anaerobic response element (ARE). Gel retardation assays were used to characterize a major, specific DNA binding protein activity found in the crude extracts. The activity is present in both aerobic and hypoxically treated cultures and has been designated ARF-B2 (ARE binding factor). ARF-B2 appears to be a multicomponent complex, with a 54 kilodalton subunit termed ARF-B2a in primary contact with the target DNA.Maize alcohol dehydrogenase-J (Adhl) is a well-studied member of a group of genes induced as part of the plant response to hypoxic stress (6,17,18 The present report details the initial characterization of the protein:DNA interactions, specific for the ARE B2, that can be detected in extracts from maize suspension cultures in order to begin to determine the molecular mechanisms that determine physiological responses to environmental stresses. MATERIALS AND METHODS Cell CulturesMaize (Zea mays L.) cell suspension cultures (line 3377 [2], provided by J. Widholm) were maintained on commercial (GIBCO) MS medium supplemented with 2 mg/L 2,4-D. For hypoxic induction, a stream of argon was bubbled through the culture medium. Whole Cell Extracts and FractionationsWhole cell protein extracts (13) were made from the cell suspensions by the methods of McKendree et al. (14). The final dialysis buffer was NEBD with 40 mM KCI. All columns and subsequent assays were conducted in NEBD buffer, with only the noted changes in KCI concentrations.For heparin agarose chromatography, the crude extract (up to 4 mL, at 2 to 5 mg total protein/ml) was applied to a 12 mL heparin agarose (Bio-Rad) column equilibrated with NEBD at 40 mM KCI at room temperature. The column was washed with NEBD at 0.1 M KCI, then the bound proteins were eluted with NEBD at 0.6 M KCI.The 0.6 M fraction was diluted with an equal volume of NEBD without KCI (to achieve a final concentration of approximately 0.3 M KCI) and applied to a Pharmacia FPLC HR 5/5 Mono Q column that had been equilibrated with NEBD at 40 mm KC1. The column was then developed with a linear gradient of40 mM KCI to 1 M KCI in NEBD. Fractions were dialyzed against NEBD at 40 mM KCI.For analytical chromatography on FPLC Superose 6 HR 10/30, solid KCI was added to crude extract to achieve 1 M, then 200 uL of the high salt extract was applied to a Superose 6 HR 10/30 column that had been equilibrated with NEBD www.plantphysiol.org on April 4, 2019 -Published by Downloaded from

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“…Nuclear proteins interacting with the G-box motif have been described previously (Giuliano et al, 1988;McKendree et al, 1990). In vitro binding experiments with the G-box motif from the Arabidopsis rbcS gene led to the identification of a nucleus-localized binding protein from tomato and Arabidopsis, which has been designated G-box binding factor (GBF) (Giuliano et al, 1988).…”

Section: Introductionmentioning

confidence: 99%

“…Recently, notable progress has been made toward understanding the molecular basis of transcriptional stimulation in plant systems. For severa1 genes, nuclear proteins have been identified that bind to regulatory DNA sequences in the promoter regions of stimuli-responsive genes (Giuliano et al, 1988;Staiger et al, 1989;McKendree et al, 1990;Schindler and Cashmore, 1990). Further characterization of these factors has been accomplished by using the DNA binding properties of the protein as a means to screen expression libraries (Mitchell and Tjian, 1989).…”

Section: Introductionmentioning

confidence: 99%

A maize protein associated with the G-box binding complex has homology to brain regulatory proteins.

1992

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The G-box element is a moderately conserved component of the promoter of many inducible genes, including the alcohol dehydrogenase genes of Arabidopsis and maize. We used monoclonal antibodies generated against partially purified G-box binding factor (GBF) activity to characterize maize proteins that are part of the DNA binding complex. Antibodies interacted with partially purified maize GBF complexes to produce a slower migrating complex in the gel retardation assay. lmmunoprecipitation experiments suggested that the protein recognized by the antibody is nota DNA binding protein in and of itself, but rather is associated with the DNA binding complex. These monoclonal antibodies were used to isolate cDNA clones encoding a protein that we have designated GF14. Maize GF14 contains a region resembling a leucine zipper and acidic carboxy and amino termini, of which the latter can form an amphipathic a-helix similar to known transcriptional activators such as VP16 and GALA. Protein gel blot analysis of cell culture extract showed that a single, major protein of approximately 30 kD is recognized by anti-GFl4; the protein is also present predominantly in the kernel and root. The deduced amino acid sequence of maize GF14 is more than 80% identical to Arabidopsis GF14 and Oenothera PHP-O, and is more than 60% identical to a class of mammalian brain proteins described as both protein kinase C inhibitors and activators of tyrosine and tryptophan hydroxylases. GF14 is found in a variety of monocotyledons and dicotyledons, gymnosperms, and yeast. This suggests a deep evolutionary conservation of a potential regulatory protein associated with a core sequence found in the promoter region of many genes.

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In vivo and in vitro characterization of protein interactions with the dyad G-box of the Arabidopsis Adh gene.

Cited by 69 publications

References 28 publications

Differential Interactions of Promoter Elements in Stress Responses of the Arabidopsis Adh Gene

Differential Interactions of Promoter Elements in Stress Responses of the Arabidopsis Adh Gene

ARF-B₂: A Protein Complex that Specifically Binds to Part of the Anaerobic Response Element of Maize Adh 1

A maize protein associated with the G-box binding complex has homology to brain regulatory proteins.

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In vivo and in vitro characterization of protein interactions with the dyad G-box of the Arabidopsis Adh gene.

Cited by 69 publications

References 28 publications

Differential Interactions of Promoter Elements in Stress Responses of the Arabidopsis Adh Gene

Differential Interactions of Promoter Elements in Stress Responses of the Arabidopsis Adh Gene

ARF-B2: A Protein Complex that Specifically Binds to Part of the Anaerobic Response Element of Maize Adh 1

A maize protein associated with the G-box binding complex has homology to brain regulatory proteins.

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ARF-B₂: A Protein Complex that Specifically Binds to Part of the Anaerobic Response Element of Maize Adh 1