Multiple interactions between nuclear proteins of Zea mays and the promoter of the Shrunken gene

Werr, Wolfgang; Springer, Boris; Schürmann, Jörg; Bellmann, Regina

doi:10.1007/bf00334705

Cited by 17 publications

(7 citation statements)

References 38 publications

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“…Nevertheless, the precise role of the dNdT stretches and datin in yeast gene transcription, DNA replication or anchoring, is currently unknown. Thus, the ES binding fraction of the NER may be related to other dNdT-rich binding factors which have been reported to interact with genes transcribed by RNA pol II in plants (Datta and Cashmore, 1989;Forde et al, 1990;Werr et a/., 1988) and, as such, could belong to a family of proteins having a more general role in the regulation of plant gene expression. The second point is that the role of the radish ES binding protein we describe here may not be restricted to transcription, as ESs from all organisms contain not only transcriptional signals but also origins of replication (Linskens and Huberman, 1988;Van't Hof et a/., 1987), replication termination sites (Hernandez etal., 1988), hot spots for recombination (Voelkel-Meiman etal., 1987) and probably binding sites for proteins which determine nucleolar structure (Reeder, 1990).…”

Section: Discussionmentioning

confidence: 99%

A nuclear protein binding to dA/dT-rich sequences upstream from the radish DMA promoter

Echeverrı́a

Delcasso-Trémousaygue

Delseny

1992

Plant J

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The external spacer (ES) of rRNA nuclear genes (rDNA) contains the sequences that control rDNA transcription initiation and enhancement. The ES is also characterized in most species by the presence of multiple repeated elements. In higher plants very few data are available on the cis- and trans-acting elements which control rDNA transcription. Using electrophoretic mobility shift assays (EMSA) it is shown that nuclear extracts from young radish leaves (NER) contain a protein fraction which binds to specific sequences in the radish ES. DNase I footprinting analysis allows mapping of the NER protein binding to dA/dT homopolymer stretches and to a 13-bp dA/dT-rich short repeat, found both in the seven approximately 100 bp repeat regions (located -1077 to -740 from transcription initiation site) and the region (-120 to -55) containing the putative promoter for rDNA transcription initiation. Whether this ES binding is due to a single or several different proteins is not known. So far, protein(s) binding to dA/dT-rich regions of a plant rDNA ES has not yet been described. Whether it is a specific RNA polymerase I transcription factor(s) or plays a more general role in genome expression remains to be elucidated.

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Section: Discussionmentioning

confidence: 99%

A nuclear protein binding to dA/dT-rich sequences upstream from the radish DMA promoter

Echeverrı́a

Delcasso-Trémousaygue

Delseny

1992

Plant J

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“…The positions of the IBP2-specific Preparation of nuclear protein extracts was performed according to Werr et al [38] except that during purification root and leaf nuclei were not collected on a 2.4 M sucrose cushion. Nuclear proteins were separated on 10~o SDS-polyacrylamide gels (37.5:1) and transferred to nitrocellulose by electroblotting.…”

Section: Northern Reverse Transcriptase Pcr and Western Blot Analysismentioning

confidence: 99%

A novel DNA-binding domain in theShrunken initiator-binding protein (IBP1)

Lugert

Werr

1994

Plant Mol Biol

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South-western screening of lambda gt11 expression library with a fragment of the Shrunken promoter containing the initiator element resulted in cloning of a novel maize gene. The encoded initiator-binding protein (IBP1) interacts at the transcription start site of the Shrunken promoter. Analysis of the 680 amino acid (aa) long polypeptide revealed a novel bipartite DNA-binding domain at the carboxyl terminus. In its amino-terminal part, it is weakly related to Myb R-repeats but the following basic region is also essential for DNA binding. A region of similarity to the conserved 2.1 and 2.2 motifs in bacterial sigma-factors is located close to the IBP1 amino terminus. Two putative nuclear localization signals are compatible with the presence of antigenically related polypeptides in nuclear protein extracts. The IBP1 gene was mapped to the long arm of chromosome 9 (9L095); a second highly related gene IBP2 is located on the short arm of chromosome 1 (1S014). Both genes encode proteins sharing 93% similarity and are transcribed with similar activity in different plant organs. A small 82 nucleotide intron in the IBP2 transcript is found unspliced to a variable degree in different tissues. Translation of this incompletely processed transcript would result in a truncated amino-terminal polypeptide lacking the DNA-binding domain.

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“…Cisacting sequences have been shown to mediate their influence on the transcription machinery via occupation by trans-acting protein factors (3). For several plant genes, nuclear factors have been identified by in vitro interaction with 5' flanking sequences (4)(5)(6)(7)(8). An in vivo function of a binding site has been demonstrated for pea nuclear factor GT-1 interacting with cis elements in the promoter region of the small subunit of the ribulose-1,5-bisphosphate carboxylase gene (9)(10)(11).…”

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A CACGTG motif of the Antirrhinum majus chalcone synthase promoter is recognized by an evolutionarily conserved nuclear protein.

Staiger¹,

Kaulen²,

Schell³

1989

Proc. Natl. Acad. Sci. U.S.A.

146

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In the chalcone synthase gene ofAntrrhinum majus (snapdragon), 150 base pairs of the 5' flanking region contain cis-acting signals for UV light-induced expression. A nuclear factor, designated CG-1, specifically recognizes a hexameric motif with internal dyad symmetry, CACGTG, located within this light-responsive sequence. Binding of CG-1 is influenced by C-methylation of the CpG dinucleotide in the recognition sequence. CG-1 is a factor found in a variety of dicotyledonous plant species including Nwotiana tabacum, A. majus, Petunia hybridla, Arabidopsis thaliana, and Glycine mar. CACGTG motifs contained within trans-acting factor recognition sites in various other plant promoters can interact with CG-1. In addition, the binding site of the human adenovirus major late transcription factor USF can compete for CG-1 binding to the chalcone synthase promoter. This suggests an evolutionary conservation of trans-acting factor recognition sites involved in divergent mechanisms of gene control.Various environmental stimuli modulate plant gene expression. Considerable information has been accumulated showing that cis-acting elements within a gene promoter are involved in light regulation, stress response, and tissuespecific and wound-induced gene expression (1,2). Cisacting sequences have been shown to mediate their influence on the transcription machinery via occupation by trans-acting protein factors (3). For several plant genes, nuclear factors have been identified by in vitro interaction with 5' flanking sequences (4-8). An in vivo function of a binding site has been demonstrated for pea nuclear factor GT-1 interacting with cis elements in the promoter region of the small subunit of the ribulose-1,5-bisphosphate carboxylase gene (9-11).We have chosen the chalcone synthase (chs) promoter of Antirrhinum majus (12) MATERIALS AND METHODSNuclear Extracts. Nuclei were prepared from 4-week-old tobacco seedlings (Nicotiana tabacum W38). The seedlings were homogenized in ice-cold NiB (25 mM Mes/KOH, pH 6/0.25 M sucrose/5 mM EDTA/10 mM KCl/0.5 mM dithiothreitol/0.5 mM phenylmethylsulfonyl fluoride) supplemented with 0.3% Nonidet P-40 and 0.5 mM spermidine using a Waring blender. The homogenate was filtered through 80-gm and 20-gm nylon mesh and the nuclei were pelleted (2000 x g; 10 min). The crude nuclear pellet was washed once with NiB/0.3% Nonidet P-40 and twice with NiB. The nuclei were resuspended in 3 vol of NEB [25 mM Hepes-KOH, pH 7.8/5% (vol/vol) glycerol/0.1 mM EGTA/420 mM KCl/0.5 mM dithiothreitol/0.5 mM phenylmethylsulfonyl fluoride/1 ,uM leupeptin/1 ,uM pepstatin]. After a brief sonication to disrupt aggregates, the suspension was stirred on ice for 45 min. After centrifugation at 100,000 x g for 45 min, the supernatant was dialyzed against 25 mM Hepes-KOH, pH 7.8/20%o (vol/vol) glycerol/0.1 mM EDTA/50 mM KCl/14 mM 2-mercaptoethanol for 2 hr and quick-frozen in liquid nitrogen. The preparation of nuclear extracts from Antirrhinum, Petunia, and Arabidopsis was done the same way. UV light irradiation of UV-...

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Multiple interactions between nuclear proteins of Zea mays and the promoter of the Shrunken gene

Cited by 17 publications

References 38 publications

A nuclear protein binding to dA/dT-rich sequences upstream from the radish DMA promoter

A nuclear protein binding to dA/dT-rich sequences upstream from the radish DMA promoter

A novel DNA-binding domain in theShrunken initiator-binding protein (IBP1)

A CACGTG motif of the Antirrhinum majus chalcone synthase promoter is recognized by an evolutionarily conserved nuclear protein.

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