Demethylation-Induced Developmental Pleiotropy in
            <b>
              <i>Arabidopsis</i>
            </b>

Ronemus, Michael; Galbiati, Massimo; Ticknor, Christine; Chen, Jychian; Dellaporta, Stephen L.

doi:10.1126/science.273.5275.654

Cited by 419 publications

(310 citation statements)

References 28 publications

Supporting

Mentioning

294

Contrasting

Unclassified

Order By: Relevance

“…4 D-H). The heterogeneity of the floral phenotype is reminiscent of phenotypes of mutants or transgenic plants affected in other chromatin modification activities, such as histone acetylation and DNA methylation (29)(30)(31). The jmj6 mutations led to the repression of OsMADS47 and DH1 (Fig.…”

Section: Discussion Specific Features Of Plant Jmjc Domain Protein Gementioning

confidence: 99%

Rice jmjC domain-containing gene JMJ706 encodes H3K9 demethylase required for floral organ development

Sun

Zhou

2008

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

163

131

View full text Add to dashboard Cite

Section: Discussion Specific Features Of Plant Jmjc Domain Protein Gementioning

confidence: 99%

Rice jmjC domain-containing gene JMJ706 encodes H3K9 demethylase required for floral organ development

Sun

Zhou

2008

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

163

131

View full text Add to dashboard Cite

“…normal development of animals 10,11 and plants [12][13][14] via effects on gene repression 15 , Xchromosome inactivation 16 , genomic imprinting 17 and replication timing 18 .…”

mentioning

confidence: 99%

The PWWP domain of mammalian DNA methyltransferase Dnmt3b defines a new family of DNA-binding folds

et al. 2002

View full text Add to dashboard Cite

The PWWP domain is a weakly conserved sequence motif found in >60 eukaryotic proteins, including the mammalian DNA methyltransferases Dnmt3a and Dnmt3b. These proteins often contain other chromatin-association domains. A 135-residue PWWP domain from mouse Dnmt3b (amino acids 223-357) has been structurally characterized at 1.8 Å resolution. The N-terminal half of this domain resembles a barrel-like five-stranded structure, whereas the C-terminal half contains a five-helix bundle. The two halves are packed against each other to form a single structural module that exhibits a prominent positive electrostatic potential. The PWWP domain alone binds DNA in vitro, probably through its basic surface. We also show that recombinant Dnmt3b2 protein (a splice variant of Dnmt3b) and two N-terminal deletion mutants (Δ218 and Δ369) have approximately equal methyl transfer activity on unmethylated and hemimethylated CpG-containing oligonucleotides. The Δ218 protein, which includes the PWWP domain, binds DNA more strongly than Δ369, which lacks the PWWP domain.Genomic patterns of cytosine methylation at the C5 position play key roles in the organization and control of mammalian chromatin (reviewed in refs 1-3). Mammalian DNA methyltransferases (MTases) all contain a C-terminal catalytic region that is structurally and functionally homologous to bacterial MTases. The eukaryotic DNA MTases have been grouped into three families based on (i) distinctive properties of their N-terminal regions and (ii) intriguing differences in DNA substrate preferences. The first eukaryotic DNA MTase, Dnmt1, contains a large N-terminal regulatory region of ~1,000 amino acids and shows a preference for hemimethylated DNA in vitro [4][5][6] . Dnmt2, a relatively small protein, contains only the MTase domain, and its function is still unclear 7 . Recombinant Dnmt3 acts on unmethylated and hemimethylated DNA at equal rates in vitro 8,9 .The task of dissecting the functional roles of the N-terminal region of the different MTase families is just beginning. These regions vary widely in size and are probably responsible for the diverse biological functions of eukaryotic DNA MTases. These functions include the © 2002 Nature Publishing Group Correspondence should be addressed to X.C. xcheng@emory.edu. Competing interests statementThe authors declare that they have no competing financial interests. HHS Public Access Dnmt3 contains a PWWP domainThe sequences of Dnmt3 orthologs have been determined from human and mouse. They all contain an N-terminal variable region (~280 amino acids in Dnmt3a and ~220 amino acids in Dnmt3b), followed by three stretches of conserved regions: the PWWP motif, six repeats of a CXXC motif and a set of 10 motifs conserved among DNA MTase catalytic regions (Fig. 1a). The PWWP motif 28 was first identified in a gene family related to the hepatomaderived growth factor (HDGF) 29 and WHSC1 genes (Wolf-Hirschhorn Syndrome Candidate) 30 . The corresponding sequence in Dnmt3 is SWWP (Fig. 1b); only the last two positions of the motif...

show abstract

“…Components involved in DNA methylation and repressive histone modification were previously identified and demonstrated to be required for transcriptional silencing (Law and Jacobsen, 2010;Matzke and Mosher, 2014;Du et al, 2015). The DNMT1-like DNA methyltransferase MET1 maintains DNA methylation at symmetric CG sites during DNA replication (Ronemus et al, 1996;Jones et al, 2001). DDM1, a SNF2-type chromatin-remodeling protein, allows DNA methyltransferases to access H1-containing heterochromatin (Zemach et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

The SUMO E3 Ligase-Like Proteins PIAL1 and PIAL2 Interact with MOM1 and Form a Novel Complex Required for Transcriptional Silencing

et al. 2016

View full text Add to dashboard Cite

The mechanism by which MORPHEUS' MOLECULE1 (MOM1) contributes to transcriptional gene silencing has remained elusive since the gene was first identified and characterized. Here, we report that two Arabidopsis thaliana PIAS (PROTEIN INHIBITOR OF ACTIVATED STAT)-type SUMO E3 ligase-like proteins, PIAL1 and PIAL2, function redundantly to mediate transcriptional silencing at MOM1 target loci. PIAL1 and PIAL2 physically interact with each other and with MOM1 to form a high molecular mass complex. In the absence of either PIAL2 or MOM1, the formation of the high molecular mass complex is disrupted. We identified a previously uncharacterized IND (interacting domain) in PIAL1 and PIAL2 and demonstrated that IND directly interacts with MOM1. The CMM2 (conserved MOM1 motif 2) domain of MOM1 was previously shown to be required for the dimerization of MOM1. We demonstrated that the CMM2 domain is also required for the interaction of MOM1 with PIAL1 and PIAL2. We found that although PIAL2 has SUMO E3 ligase activity, the activity is dispensable for PIAL2's function in transcriptional silencing. This study suggests that PIAL1 and PIAl2 act as components of the MOM1-containing complex to mediate transcriptional silencing at heterochromatin regions.

show abstract

Demethylation-Induced Developmental Pleiotropy in Arabidopsis

Cited by 419 publications

References 28 publications

Rice jmjC domain-containing gene JMJ706 encodes H3K9 demethylase required for floral organ development

Rice jmjC domain-containing gene JMJ706 encodes H3K9 demethylase required for floral organ development

The PWWP domain of mammalian DNA methyltransferase Dnmt3b defines a new family of DNA-binding folds

The SUMO E3 Ligase-Like Proteins PIAL1 and PIAL2 Interact with MOM1 and Form a Novel Complex Required for Transcriptional Silencing

Contact Info

Product

Resources

About