High impact information on Emp3

• Here, we compared sequence and systematically mapped position of DNase I hypersensitive sites, acetylation status of histone H3/H4, and in vivo binding of transcription factors over approximately 120 kilobases flanking the human GATA1 gene and the corresponding region in mice [1].
• Cell cycle regulation of a mouse histone H4 gene requires the H4 promoter [2].
• The mouse histone H4 gene, when stably transformed into L cells on the PSV2gpt shuttle vector, is cell cycle regulated in parallel with the endogenous H4 genes [2].
• The IFN regulatory factor-2 (IRF-2) oncoprotein controls the cell cycle-dependent expression of histone H4 genes during S phase and may function as a component of an E2F-independent mechanism to regulate cell growth [3].
• Extending the study, we found that histones H1, H2A, H2B, H3, and H4 from calf thymus are all able to bind LPS [4].

Biological context of Emp3

• Tmp was mapped to mouse chromosome 6, Xmp was mapped to chromosome 16, and Ymp was mapped to chromosome 7 [5].
• A single nucleotide polymorphism in the Emp3 gene defines the H4 minor histocompatibility antigen [6].
• These results provide a molecular mechanism for the H4 minor H antigen and suggest a novel mechanism by which alloantigenic disparity caused by conservative amino acid changes can be augmented by posttranslational antigen processing events [6].
• Maximal increases in histone H4 acetylation over the promoter and intron 1 region were seen within 10 min of HDAC inhibition, while the increases seen on the 3' end showed slower kinetics [7].
• Sequencing of EMP-3 revealed an SNP leading to an amino acid substitution (p.T153I) that was found in all mouse strains susceptible for DCC but not in resistant strains such as C57BL/6 mice [8].

Anatomical context of Emp3

• Both also reacted with liver, H-4 recognizing antigen present on the hepatocyte, and H-13 recognizing antigen distributed along the sinusoid [9].
• In the human fetal kidney, H-13 reacted with the mesangium, glomerular and tubular basement membrane and Bowman's capsule, and H-4 with the glomerular and tubular epithelial cells [9].

Associations of Emp3 with chemical compounds

• Surprisingly, the widely used inhibitor trichostatin A (TSA) had little (cycling cells) or no (quiescent cells) effect on H4 acetylation in CD34+ UBC [10].
• Bindings were specific, and affinities, determined by isothermal titration calorimetry, were (except for H4) higher than that of the LPS-binding antibiotic polymyxin B [4].
• Immunoblot analysis of 2.0 M guanidine HCl extract after dissociation in sodium dodecyl sulfate and electrophoresis demonstrated binding of H-4 to a 125 kd polypeptide [9].
• Affinity chromatography of rod domains of IF proteins on core histone-Sepharose 4B and of histones and their limit peptides on vimentin-Sepharose 4B has shown that the interactions involving fractions of histones H3 and H4 are extremely resistant to salt and can be dissociated only with arginine or salt under denaturing conditions [11].

Analytical, diagnostic and therapeutic context of Emp3

• G-CSF caused rapid acetylation of histone H3 and H4 at the promoter of MPO as revealed by chromatin immunoprecipitation [12].

References