Key Spec Table
|Species Reactivity||Key Applications||Host||Format||Antibody Type|
|H, Yeast (S. cerevisiae)||IP, WB, ICC||Rb||Purified||Polyclonal Antibody|
|Description||Anti-MYST family Antibody|
|Presentation||0.7M Tris-glycine, pH 7.4, 0.105M NaCl, 0.035% azide containing 30% glycerol|
|Application||Use Anti-MYST family Antibody (Rabbit Polyclonal Antibody) validated in IP, WB, ICC to detect MYST family also known as K-Acetyltransferase, KAT.|
|Safety Information according to GHS|
|Storage and Shipping Information|
|Storage Conditions||2 years at -20°C|
|Material Size||200 µg|
|Anti-MYST family - 17603||17603|
|Reference overview||Application||Pub Med ID|
|F-actin-dependent insolubility of chromatin-modifying components.|
Andrin, C; Hendzel, MJ
The Journal of biological chemistry 279 25017-23 2004
Many complexes involved in chromatin modification are difficult to isolate and commonly found associated with nuclear matrix preparations. In this study, we examine the elution properties of chromatin-modifying components under different extraction conditions. We find that most, but not all, histone acetyltransferases and histone deacetylases predominantly partition with the nuclear pellet during intermediate salt extraction. In attempts to identify a biological basis for the observed insolubility, we demonstrate that depolymerizing cellular actin, but not cellular tubulin, mobilizes a significant proportion of the insoluble pool into the intermediate salt-soluble nuclear extract. The disruption of cellular F-actin releases a specific subset of high molecular weight, active, nuclear histone deacetylase complexes that are not found under normal conditions. This study demonstrates that actin polymerization, a physiologically relevant process, is responsible for the observed insolubility of these components during nuclear extract preparation and establishes a simple strategy for isolating subsets of chromatin-modifying complexes that are otherwise depleted or absent under the same extraction conditions.
|Analysis of mammalian proteins involved in chromatin modification reveals new metaphase centromeric proteins and distinct chromosomal distribution patterns|
Craig, J. M., et al
Hum Mol Genet, 12:3109-21 (2003) 2003
|ESA1 is a histone acetyltransferase that is essential for growth in yeast.|
Smith, E R, et al.
Proc. Natl. Acad. Sci. U.S.A., 95: 3561-5 (1998) 1998
Posttranslational acetylation of core histone amino termini has long been associated with transcriptionally active chromatin. Recent reports have demonstrated histone acetyltransferase activity in a small group of conserved transcriptional regulators directly linked to gene activation. In addition, the presence of a putative acetyltransferase domain has been discovered in a group of proteins known as the MYST family (for its founding members MOZ, YBF2/SAS3, SAS2, and Tip60). Members of this family are implicated in acute myeloid leukemia (MOZ), transcriptional silencing in yeast (SAS2 and YBF2/SAS3), HIV Tat interaction in humans (Tip60), and dosage compensation in Drosophila (MOF). In this report, we express a yeast ORF with homology to MYST family members and show it possesses histone acetyltransferase activity. Unlike the other MYST family members in Saccharomyces cerevisiae this gene is essential for growth.
|mof, a putative acetyl transferase gene related to the Tip60 and MOZ human genes and to the SAS genes of yeast, is required for dosage compensation in Drosophila.|
Hilfiker, A, et al.
EMBO J., 16: 2054-60 (1997) 1997
Dosage compensation is a regulatory process that insures that males and females have equal amounts of X-chromosome gene products. In Drosophila, this is achieved by a 2-fold enhancement of X-linked gene transcription in males, relative to females. The enhancement of transcription is mediated by the activity of a group of regulatory genes characterized by the male-specific lethality of their loss-of-function alleles. The products of these genes form a complex that is preferentially associated with numerous sites on the X chromosome in somatic cells of males but not of females. Binding of the dosage compensation complex is correlated with a significant increase in the presence of a specific histone isoform, histone 4 acetylated at Lys16, on this chromosome. Experimental results and sequence analysis suggest that an additional gene, males-absent on the first (mof), encodes a putative acetyl transferase that plays a direct role in the specific histone acetylation associated with dosage compensation. The predicted amino acid sequence of MOF exhibits a significant level of similarity to several other proteins, including the human HIV-1 Tat interactive protein Tip60, the human monocytic leukemia zinc finger protein MOZ and the yeast silencing proteins SAS3 and SAS2.
|Novel substrate specificity of the histone acetyltransferase activity of HIV-1-Tat interactive protein Tip60.|
Yamamoto, T and Horikoshi, M
J. Biol. Chem., 272: 30595-8 (1997) 1997
Tip60, originally isolated as an HIV-1-Tat interactive protein, contains an evolutionarily conserved domain with yeast silencing factors. We demonstrate here direct biochemical evidence that this domain of Tip60 has histone acetyltransferase activity. The purified recombinant effectively acetylates H2A, H3, and H4 but not H2B of core histone mixtures. This substrate specificity has not been observed among histone acetyltransferases analyzed to date. These results indicate that Tip60 is a histone acetyltransferase with a novel property, suggesting that Tip60 and its related factors may introduce a distinct alteration on chromatin.
|The role of Sas2, an acetyltransferase homologue of Saccharomyces cerevisiae, in silencing and ORC function.|
Ehrenhofer-Murray, A E, et al.
Genetics, 145: 923-34 (1997) 1997
Silencing at the cryptic mating-type loci HML and HMR of Saccharomyces cerevisiae requires regulatory sites called silencers. Mutations in the Rap1 and Abf1 binding sites of the HMR-E silencer (HMRa-e**) cause the silencer to be nonfunctional, and hence, cause derepression of HMR. Here, we have isolated and characterized mutations in SAS2 as second-site suppressors of the silencing defect of HMRa-e**. Silencing conferred by the removal of SAS2 (sas2 delta) depended upon the integrity of the ARS consensus sequence of the HMR-E silencer, thus arguing for an involvement of the origin recognition complex (ORC). Restoration of silencing by sas2 delta required ORC2 and ORC5, but not SIR1 or RAP1. Furthermore, sas2 delta suppressed the temperature sensitivity, but not the silencing defect of orc2-1 and orc5-1. Moreover, sas2 delta had opposing effects on silencing of HML and HMR. The putative Sas2 protein bears similarities to known protein acetyltransferases. Several models for the role of Sas2 in silencing are discussed.