Brain proteins in plants: an Arabidopsis homolog to neurotransmitter pathway activators is part of a DNA binding complex.

Lu, Ge; DeLisle, Alice J.; Vetten, Nick C. de; Ferl, Robert J.

doi:10.1073/pnas.89.23.11490

Cited by 158 publications

(178 citation statements)

References 44 publications

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“…Since these assays are carried out under non-denaturing conditions, it is possible that additional, negatively charged proteins are associated with GBF in the nuclear extract such that a faster migrating complex is formed. We note that the previously described GF14 protein that appears to be associated with GBF is highly acidic (de Vetten et al, 1992).…”

Section: Binding-site Sequence Specificity Of Gbf Imentioning

confidence: 56%

“…A specific DNA-protein complex was formed with extracts from E.colicarrying the GBF1 expression vector, and that complex was effectively competed when the dyad G-box oligonucleotide was included in the binding reaction ( Figure 6b, lanes 2 and 3). No complexes were formed with control E. coil protein extracts from cells carrying pET-GF14 (lanes 4 and 5), suggesting that bacteria have no proteins with G-box binding affinity in this assay and demonstrating further that GF14 protein is not a G-box DNA binding factor in and of itself (de Vetten et aL, 1992).…”

Section: Binding-site Sequence Specificity Of Gbf Imentioning

confidence: 83%

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Characterization of a maize G‐box binding factor that is induced by hypoxia

Vetten¹,

Ferl²

1995

The Plant Journal

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SummaryG-box cis-acting DNA sequence elements are present in the promoter region of a number of signal-inducible plant genes. In many cases this motif is essential for gene expression. Maize nuclear extracts contain a protein complex that binds specifically to the G-box sequence. Previously, a protein called GF14 was described that is physically associated with the G-box binding complex, but is not a DNA-binding factor in and of itself. This paper reports the isolation of a cDNA encoding a maize G-box binding factor (GBF). The deduced amino acid sequence indicates that maize GBF1 is a basic region-leucine zipper protein. GBF1 binds to the G-box element with specificity similar to that of the binding activity in nuclear extracts. Furthermore, maize GBF1 and the factor detected in nuclear extract are identical in their molecular weight and are immunologicelly related. GBF1 mRNA accumulates rapidly in hypoxicelly induced maize cells prior to the increase in Adhl mRNA levels. Taken together with results that indicate that GBF1 binds to the hypoxia-responsive promoter of maize Adh 1, these observations suggest that GBF1 may be one of the factors involved in the activation of Adh l.

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Section: Binding-site Sequence Specificity Of Gbf Imentioning

confidence: 56%

Section: Binding-site Sequence Specificity Of Gbf Imentioning

confidence: 83%

Characterization of a maize G‐box binding factor that is induced by hypoxia

Vetten¹,

Ferl²

1995

The Plant Journal

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“…A monoclonal antibody raised against GF14, a 14-3-3 protein from A. thaliuna [18], demonstrated the existence of 14-3-3 homologs in both, the soluble and the microsomal, fractions from leaves of C. communis. The antibody exclusively recognized a doublett of polypeptides of approximately 31 and 32 kDa in those crude fractions, confirming its specificity and applicability for C. communis (not shown).…”

Section: Resultsmentioning

confidence: 99%

“…Immunoblot analysis was carried out as in [17]. The monoclonal antibody raised against GF14 [18], a 14-3-3 protein from A. thaliana (antibody GF14-19, kindly provided by Dr. R.J. Ferl, Gainesville, USA), was used at a final dilution of 1: 5,000. The antiserum against the A. thaliana H'-ATPase was kindly provided by Dr. R. Serrano, Valencia, Spain, and was used at a final dilution of l:lO,OOO.…”

Section: Methodsmentioning

confidence: 99%

The fusicoccin receptor of plants is a member of the 14‐3‐3 superfamily of eukaryotic regulatory proteins

1994

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The receptor for the wilt-inducing phytotoxin fusicoccin was purified to homogeneity from plasma membranes of Commelina communis as a complex with the radioligand [3H]9'-nor-8'-hydroxyfusicoccin. The preparation consisted of two polypeptides with apparent molecular masses of 30.5 kDa and 31.5 kDa and with isoelectric points of around pH 5.2 and 5.3, respectively. The proteins were N-terminally blocked. Internal amino acid sequences were obtained for both polypeptides of the fusicoccin-binding complex. Sequence information, as well as subsequent immunological analysis, proved that both polypeptides are members of the eukaryotic 143-3 family, which comprises structurally conserved regulatory proteins of widespread occurrence and a wide range of functions. 143-3 isoform(s) constituting the fusicoccin receptor are distinguishable from other cellular 143-3 proteins by their tight association with the plasma membrane. Applying temperature-induced Triton X-l 14 phase separation experiments, they, as well as the target enzyme of fusicoccin action, the H'-ATPase, partitioned into the phospholipid-rich fraction which contains the most hydrophobic proteins. The results discussed herein provide a basis for the elucidation of the molecular mechanism of fusicoccin action.

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“…In these non-mammalian species, a variety of roles for regulation of gene expression have been suggested, (reviewed in [4]). More recently, additional evidence for a role in regulation of transcription has come from the group of Ferl [17] who have shown that a plant 14-3-3 homologue binds to the G-box promoter element of inducible genes. In some mammalian tissues, novel isoforms may be expressed at high level.…”

Section: Introductionmentioning

confidence: 99%

Antibodies against the major brain isofbrms of 14‐3‐3 protein

Martin¹,

Patel²,

Jones³

et al. 1993

FEBS Letters

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14-3-3 proteins are apparently ubiquitous eukaryotic proteins that comprise a large number of isoforms. They have been implicated in the regulation of a wide range of biological processes [reviewed in Aitken et al. (1992) Trends B&hem. Sci. 17,498-5011. We have raised specific antibodies against each mammalian brain isoform of 14-3-3 employing peptides synthesised from the amino-terminal regions. The peptides were, like the proteins from mammalian brain, N-acetylated. The antiserum specific for the epsilon isofonn did not recognise the recombinant form of this protein (lacking the N-acetyl co-translational modification) expressed in E. coli until it was chemically acetylated.

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Brain proteins in plants: an Arabidopsis homolog to neurotransmitter pathway activators is part of a DNA binding complex.

Abstract: The G box is a well-characterized cis-acting

Cited by 158 publications

References 44 publications

Characterization of a maize G‐box binding factor that is induced by hypoxia

Characterization of a maize G‐box binding factor that is induced by hypoxia

The fusicoccin receptor of plants is a member of the 14‐3‐3 superfamily of eukaryotic regulatory proteins

Antibodies against the major brain isofbrms of 14‐3‐3 protein

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