Self-association of the SET domains of human ALL-1 and of Drosophila TRITHORAX and ASH1 proteins

Rozovskaia, Tanya; Rozenblatt-Rosen, Orit; Sedkov, Yurii; Burakov, Darya; Yano, Takahiro; Nakamura, Tatsuya; Petruck, S; Ben-Simchon, Levana; Croce, Carlo M.; Mazo, Alexander; Canaani, Eli

doi:10.1038/sj.onc.1203307

Cited by 41 publications

(32 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…One of them is the MLL SET domain itself, showing the ability to homo-dimerize [Rozovskaia et al, 2000]. Another protein that interacts with the carboxyl-terminus of MLL is hSNF5, a member of the SWI/SNF protein complex that functions in chromatin remodeling [Rozenblatt-Rosen et al, 1998].…”

Section: Many Pieces Of the Puzzlementioning

confidence: 99%

MLL: How complex does it get?

Popovic

Zeleznik‐Le

2005

J of Cellular Biochemistry

View full text Add to dashboard Cite

The mixed lineage leukemia (MLL) gene encodes a very large nuclear protein homologous to Drosophila trithorax (trx). MLL is required for the proper maintenance of HOX gene expression during development and hematopoiesis. The exact regulatory mechanism of HOX gene expression by MLL is poorly understood, but it is believed that MLL functions at the level of chromatin organization. MLL was identified as a common target of chromosomal translocations associated with human acute leukemias. About 50 different MLL fusion partners have been isolated to date, and while similarities exist between groups of partners, there exists no unifying property shared by all the partners. MLL gene rearrangements are found in leukemias with both lymphoid and myeloid phenotypes and are often associated with infant and secondary leukemias. The immature phenotype of the leukemic blasts suggests an important role for MLL in the early stages of hematopoietic development. Mll homozygous mutant mice are embryonic lethal and exibit deficiencies in yolk sac hematopoiesis. Recently, two different MLL-containing protein complexes have been isolated. These and other gain-and loss-of-function experiments have provided insight into normal MLL function and altered functions of MLL fusion proteins. This article reviews the progress made toward understanding the function of the wild-type MLL protein. While many advances in understanding this multifaceted protein have been made since its discovery, many challenging questions remain to be answered. J. Cell. Biochem. 95: 234-242, 2005. ß 2005 Wiley-Liss, Inc.

show abstract

Section: Many Pieces Of the Puzzlementioning

confidence: 99%

MLL: How complex does it get?

Popovic

Zeleznik‐Le

2005

J of Cellular Biochemistry

View full text Add to dashboard Cite

show abstract

“…At least some SET proteins are capable of self-association [103][104][105]. This property suggests that the lysine-methyltransferase activity, including varying degrees of methylation (mono-, di-or tri-methylation), substrate specificity and localization can be subjected to regulation by intra-and inter-molecular interactions with other proteins.…”

Section: Regulation Of Set Protein Functions Through Protein-protein mentioning

confidence: 99%

“…The possibility also exists that SET protein isoforms resulting from alternative splicing assemble into higher order protein complexes. Homodimerization or heterodimerization has been reported for the virus SET protein vSET [135], human G9a, and GLP [136], and Drosophila ASH1 and Trx [105]. If plant SET proteins form dimers, alternative splicing of SET genes could generate proteins forming various homo-and hetero-dimers having distinct biological activities.…”

Section: Alternative Splicing Of Arabidopsis Set Genesmentioning

confidence: 99%

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

Wang

Chandrasekharan

et al. 2007

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

176

195

View full text Add to dashboard Cite

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.

show abstract

“…In contrast, control yeast containing individual constructs did not activate reporter expression. Although MEA was shown to bind weakly to itself ( Figure 1E), analogous to the selfassociation of SET domain polypeptides in Drosophila and human (Rozovskaia et al, 2000), no other strong interactions, including pairwise combinations with FIS2, were detected in the yeast two-hybrid experiments (Figure 1). Therefore, these results suggest that the FIE and MEA proteins interact specifically in a yeast two-hybrid system.…”

Section: Fie and Mea Proteins Interactmentioning

confidence: 99%

Mutations in the FIE and MEA Genes That Encode Interacting Polycomb Proteins Cause Parent-of-Origin Effects on Seed Development by Distinct Mechanisms

et al. 2000

View full text Add to dashboard Cite

In flowering plants, two cells are fertilized in the haploid female gametophyte. Egg and sperm nuclei fuse to form the embryo. A second sperm nucleus fuses with the central cell nucleus, which replicates to generate the endosperm, a tissue that supports embryo development. The FERTILIZATION-INDEPENDENT ENDOSPERM ( FIE ) and MEDEA ( MEA ) genes encode WD and SET domain polycomb proteins, respectively. In the absence of fertilization, a female gametophyte with a loss-of-function fie or mea allele initiates endosperm development without fertilization. fie and mea mutations also cause parent-of-origin effects, in which the wild-type maternal allele is essential and the paternal allele is dispensable for seed viability. Here, we show that FIE and MEA polycomb proteins interact physically, suggesting that the molecular partnership of WD and SET domain polycomb proteins has been conserved during the evolution of flowering plants. The overlapping expression patterns of FIE and MEA are consistent with their suppression of gene transcription and endosperm development in the central cell as well as their control of seed development after fertilization. Although FIE and MEA interact, differences in maternal versus paternal patterns of expression, as well as the effect of a recessive mutation in the DECREASE IN DNA METHYLATION1 ( DDM1 ) gene on mutant allele transmission, indicate that fie and mea mutations cause parent-of-origin effects on seed development by distinct mechanisms. INTRODUCTIONFlowering plant reproduction involves fertilization of two cells (reviewed in van Went and Willemse, 1984). Within the Arabidopsis ovule, the female gametophyte consists of an egg cell and two synergid cells at the micropylar end, a central cell in the middle, and three antipodal cells at the chalazal end. All are haploid except for the central cell, which contains two polar nuclei that fuse to form a diploid nucleus. Reproduction is initiated when an entering pollen tube discharges two genetically identical haploid sperm cells. Fertilization of the egg generates the diploid embryo, which passes through morphologically defined stages (globular, heart, torpedo, walking stick, early maturation, and maturation) (Goldberg et al., 1994;Jurgens and Mayer, 1994). During embryo development, two organ systems (axis and cotyledon) and three tissue layers (protoderm, procambium, and ground meristem) are specified (Lindsey and Topping, 1993;Jurgens, 1994;Meinke, 1994).Fertilization of the central cell generates the triploid endosperm, for which the pattern of development differs dramatically from that of the embryo. Arabidopsis endosperm development is characteristic of nuclear endosperm development in angiosperms (Mansfield and Briarty, 1990a;Webb and Gunning, 1991;Berger, 1999;Brown et al., 1999). The Arabidopsis primary endosperm nucleus replicates without cytokinesis to form a syncytium of nuclear-cytoplasmic domains that migrate to the periphery of the expanding central cell (Brown et al., 1999). When the embryo is at the globular/heart transi...

show abstract

Self-association of the SET domains of human ALL-1 and of Drosophila TRITHORAX and ASH1 proteins

Cited by 41 publications

References 23 publications

MLL: How complex does it get?

MLL: How complex does it get?

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

Mutations in the FIE and MEA Genes That Encode Interacting Polycomb Proteins Cause Parent-of-Origin Effects on Seed Development by Distinct Mechanisms

Contact Info

Product

Resources

About