title: Physical and functional interactions of histone deacetylase 3 with TFII-I family proteins and PIASxbeta.
abstract: TFII-I family proteins are characterized structurally by the presence of multiple reiterated I-repeats, each containing a putative helix-loop-helix domain. Functionally, they behave as multifunctional transcription factors that are activated by a variety of extracellular signals. In studying their subcellular localization, we noticed that these transcription factors frequently reside in subnuclear domains/dots. Because nuclear dots are believed often to harbor components of histone deacetylase enzymes (HDACs), we investigated whether TFII-I family proteins colocalize and interact with HDACs. Here, we show that TFII-I and its related member hMusTRD1/BEN physically and functionally interact with HDAC3. The TFII-I family proteins and HDAC3 also show nearly identical expression patterns in early mouse development. Consistent with our earlier observation that TFII-I family proteins also interact with PIASxbeta, a member of the E3 ligase family involved in the small ubiquitin-like modifier (SUMO) pathway, we show further that PIASxbeta physically and functionally interacts with HDAC3 and relieves the transcriptional repression exerted by HDAC3 upon TFII-I-mediated gene activation. These results suggest a complex interplay between two posttranslational pathways-histone modification and SUMOylation-brokered in part by TFII-I family proteins.
authors.affiliation: Department of Pathology, Tufts University School of Medicine, 136 Harrison Avenue, Boston, MA 02111, USA.
authors.forename: María Isabel
authors.initials: MI
authors.lastname: Tussié-Luna
authors.forename: Dashzeveg
authors.initials: D
authors.lastname: Bayarsaihan
authors.forename: Edward
authors.initials: E
authors.lastname: Seto
authors.forename: Frank H
authors.initials: FH
authors.lastname: Ruddle
authors.forename: Ananda L
authors.initials: AL
authors.lastname: Roy
mesh_terms: D000818:Animals; D019556:COS Cells; D004247:DNA / Q000378:metabolism; D005786:Gene Expression Regulation; D017930:Genes, Reporter; D049452:Green Fluorescent Proteins; D006655:Histone Deacetylases / Q000378:metabolism*; D007150:Immunohistochemistry; D008025:Ligases / Q000378:metabolism; D008156:Luciferases / Q000378:metabolism; D008164:Luminescent Proteins / Q000378:metabolism; D008856:Microscopy, Fluorescence; D010957:Plasmids / Q000378:metabolism; D011233:Precipitin Tests; D011485:Protein Binding; D020033:Protein Isoforms; D011499:Protein Processing, Post-Translational; D014158:Transcription, Genetic; D015533:Transcriptional Activation; D014162:Transfection; D020798:Two-Hybrid System Techniques; D044767:Ubiquitin-Protein Ligases; D000099186:Histone Deacetylase 3
chemical_list: D004247:DNA; D049452:Green Fluorescent Proteins; D006655:Histone Deacetylases; D008025:Ligases; D008156:Luciferases; D008164:Luminescent Proteins; D020033:Protein Isoforms; D044767:Ubiquitin-Protein Ligases; D000099186:Histone Deacetylase 3