β-Phaseolin gene activation is a two-step process: PvALF- facilitated chromatin modification followed by abscisic acid-mediated gene activation

Li, Guofu; Bishop, Kenneth J.; Chandrasekharan, Mahesh B.; Hall, Timothy C.

doi:10.1073/pnas.96.12.7104

Cited by 67 publications

(58 citation statements)

References 43 publications

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“…Hall, unpublished data) and PvALF (Phaseolus vulgaris ABI3-like factor) [77][78][79]. In addition, an increase in H3K4me 3 at the phas chromatin was detected within one hour upon phas activation, illustrating the dynamic aspects of chromatin remodeling in mediating the activation of this seed-specific promoter [79].…”

Section: Class Iii: the Trithorax Homologs And Related Proteins (H3k4)mentioning

confidence: 93%

Plant SET domain-containing proteins: Structure, function and regulation

Wang

Chandrasekharan

et al. 2007

Biochimica et Biophysica Acta (BBA) - Gene Structure and Expres

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176

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Modification of the histone proteins that form the core around which chromosomal DNA is looped has profound epigenetic effects on the accessibility of the associated DNA for transcription, replication and repair. The SET domain is now recognized as generally having methyltransferase activity targeted to specific lysine residues of histone H3 or H4. There is considerable sequence conservation within the SET domain and within its flanking regions. Previous reviews have shown that SET proteins from Arabidopsis and maize fall into five classes according to their sequence and domain architectures. These classes generally reflect specificity for a particular substrate. SET proteins from rice were found to fall into similar groupings, strengthening the merit of the approach taken. Two additional classes, VI and VII, were established that include proteins with truncated/ interrupted SET domains. Diverse mechanisms are involved in shaping the function and regulation of SET proteins. These include protein-protein interactions through both intra-and inter-molecular associations that are important in plant developmental processes, such as flowering time control and embryogenesis. Alternative splicing that can result in the generation of two to several different transcript isoforms is now known to be widespread. An exciting and tantalizing question is whether, or how, this alternative splicing affects gene function. For example, it is conceivable that one isoform may debilitate methyltransferase function whereas the other may enhance it, providing an opportunity for differential regulation. The review concludes with the speculation that modulation of SET protein function is mediated by antisense or sense-antisense RNA.

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Section: Class Iii: the Trithorax Homologs And Related Proteins (H3k4)mentioning

confidence: 93%

Plant SET domain-containing proteins: Structure, function and regulation

Wang

Chandrasekharan

et al. 2007

Biochimica et Biophysica Acta (BBA) - Gene Structure and Expres

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176

195

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“…For example, a histone methyltransferase equipped with a CW domain has recently been shown to regulate flowering in Arabidopsis . Intriguingly, chromatin remodeling has been implicated in gene regulation mediated by other B3 domain factors, including ABI3 (Li et al, 1999;Levy et al, 2002;Fukaki et al, 2006;Ng et al, 2006), with association of PKL function (Fukaki et al, 2006). Hence, VAL B3 factors may associate with general chromatin factors, perhaps as part of the protein complex, to repress expression of a specific set of genes.…”

Section: Discussionmentioning

confidence: 99%

Repression of theLEAFY COTYLEDON 1/B3Regulatory Network in Plant Embryo Development byVP1/ABSCISIC ACID INSENSITIVE 3-LIKEB3 Genes

2006

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Plant embryo development is regulated by a network of transcription factors that include LEAFY COTYLEDON 1 (LEC1), LEC1-LIKE (L1L), and B3 domain factors, LEAFY COTYLEDON 2 (LEC2), FUSCA3 (FUS3), and ABSCISIC ACID INSENSITIVE 3 (ABI3) of Arabidopsis (Arabidopsis thaliana). Interactions of these genes result in temporal progression of overlapping B3 gene expression culminating in maturation and desiccation of the seed. Three VP1/ABI3-LIKE (VAL) genes encode B3 proteins that include plant homeodomain-like and CW domains associated with chromatin factors. Whereas val monogenic mutants have phenotypes similar to wild type, val1 val2 double-mutant seedlings form no leaves and develop embryo-like proliferations in root and apical meristem regions. In a val1 background, val2 and val3 condition a dominant variegated leaf phenotype revealing a VAL function in vegetative development. Reminiscent of the pickle (pkl) mutant, inhibition of gibberellin biosynthesis during germination induces embryonic phenotypes in val1 seedlings. Consistent with the embryonic seedling phenotype, LEC1, L1L, ABI3, and FUS3 are up-regulated in val1 val2 seedlings in association with a global shift in gene expression to a profile resembling late-torpedo-stage embryogenesis. Hence, VAL factors function as global repressors of the LEC1/B3 gene system. The consensus binding site of the ABI3/FUS3/LEC2 B3 DNA-binding domain (Sph/RY) is strongly enriched in the promoters and first introns of VAL-repressed genes, including the early acting LEC1 and L1L genes. We suggest that VAL targets Sph/RY-containing genes in the network for chromatin-mediated repression in conjunction with the PKLrelated CHD3 chromatin-remodeling factors.

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“…This is achieved by a repressive chromatin architecture (17) that is remodeled concomitant with gene activation in the developing seed, resulting in disruption of histone-mediated DNA wrapping and permitting abundant factor binding to the phas promoter (18). Activation of the phas promoter is a two-step process: chromatin modification mediated by the transcription factor PvALF, followed by abscisic acid (ABA)-mediated transcriptional activation (19).…”

mentioning

confidence: 99%

“…19) and line PvAlf-14 plants (a 58.1A plant retransformed with CaMV35S/PvAlf, see Ref. 19) and bean leaves were treated with protein synthesis inhibitors.…”

mentioning

confidence: 99%

“…19) and line PvAlf-14 plants (a 58.1A plant retransformed with CaMV35S/PvAlf, see Ref. 19) and bean leaves were treated with protein synthesis inhibitors. To our surprise, we found that three potent eukaryotic protein synthesis inhibitors (CHX, verrucarin A, and emetine) were able to induce transcriptional expression from the phas promoter in these vegetative tissues without the presence of either PvALF or ABA.…”

mentioning

confidence: 99%

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De Novo Activation of the β-Phaseolin Promoter by Phosphatase or Protein Synthesis Inhibitors

Li¹,

Bishop

Hall

2001

Journal of Biological Chemistry

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The promoter for the phaseolin (phas) bean seed protein gene adopts an inactive chromatin structure in leaves of transgenic tobacco. This repressive architecture, which confers stringent spatial regulation, is disrupted upon transcriptional activation during embryogenesis in a process that requires the presence of both a transcription factor (PvALF) and abscisic acid (ABA). Toward determining the need for de novo synthesis of proteins other than PvALF in transcriptional activation we explored the effect of several eukaryotic protein synthesis inhibitors. Surprisingly, cycloheximide (CHX), emetine, and verrucarin A were able to induce transcription from the phas promoter in tobacco and bean leaf tissue in the absence of either PvALF or ABA. This induction was decreased by the replication inhibitors hydroxyurea and aphidicolin but not by genistein or mimosine. Since protein phosphatases and kinases are essential components of the ABA signal transduction pathway, it is conceivable that CHX is also capable of inducing phosphorylation of proteins usually involved in ABA-mediated activation. Interestingly, okadaic acid, an inhibitor of serine/threonine phosphatase, also strongly activated transcription from the phas promoter. In contrast, the protein synthesis inhibitors anisomycin and puromycin did not activate transcription from the phas promoter, nor did the tyrosine phosphatase inhibitors phenylarsine oxide and sodium orthovanadate. These discrete but different results on transcriptional activation may reflect specific modes of action of the inhibitors, or they may reflect differential interactions of the inhibitors or of downstream events resulting from inhibitor activity with presently unknown components of the transcriptional activation system.

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β-Phaseolin gene activation is a two-step process: PvALF- facilitated chromatin modification followed by abscisic acid-mediated gene activation

Cited by 67 publications

References 43 publications

Plant SET domain-containing proteins: Structure, function and regulation

Plant SET domain-containing proteins: Structure, function and regulation

Repression of theLEAFY COTYLEDON 1/B3Regulatory Network in Plant Embryo Development byVP1/ABSCISIC ACID INSENSITIVE 3-LIKEB3 Genes

De Novo Activation of the β-Phaseolin Promoter by Phosphatase or Protein Synthesis Inhibitors

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