Disease relevance of TBPL1

• DNA sequences coding for alpha globin genes are preferentially represented in the TBP-associated DNA fractions isolated from erythroid cells (erythroblasts, mature erythrocytes, differentiated and non-differentiated Friend erythroleukemia cells), but not from cultured fibroblast cells [1].

High impact information on TBPL1

• We propose that the developmental regulation of beta-globin expression is achieved, in part, by the requirement of an erythroid protein and a stage-specific factor, rather than TBP, to activate chromatin through a specialized TATA box [2].
• In transcriptionally active nuclei, complexes of TBP interact with the nuclear matrix, while in mature erythrocytes this interaction disappears [1].
• Distribution of proteins tightly bound to DNA (TBP) along the DNA chain was found to depend on the cell lineage [1].
• Also, TEF-1 acts as a transcriptional repressor in placental cells, possibly through interaction with the TATA binding protein (TBP), preventing TBP binding to the TATA box [3].
• These results suggest a random distribution of the TBP in that genome, due possibly to a transient interaction between DNA and TBP [4].

Biological context of TBPL1

• Liquid hybridization of nick-translation-labeled DNA-TBP with a large excess of total chicken nuclear DNA also demonstrated that the DNA is not a specific subset of the genome [4].

Anatomical context of TBPL1

• In the nuclei from laying hen oviducts in which the ovalbumin gene but not the globin is actively expressed, approximately 3-fold enrichment of the ovalbumin gene was found in the DNA-TBP [4].

Analytical, diagnostic and therapeutic context of TBPL1

• The ovalbumin gene sequences in the DNA-TBP were analyzed by the Southern blot [4].

References