Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P20226 (TATA-binding protein)
 1,297 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We investigated high density lipoprotein (HDL) subfractions in abetalipoproteinemia (ABL) using rate zonal ultracentrifugation. In ABL, HDL2 is the major subfraction, 65% of total mass compared to less than 10% in normal subjects with similar HDL levels. HDL2 and HDL3 in ABL (n = 3) are larger and lighter than in normals (n = 3), with mean diameters of 136 +/- 19 A and 100 +/- 12 A, respectively (as compared to 113 +/- 12 A and 86 +/- 11 A), and contained more apoprotein E. ABL-HDL2 and HDL3 particles contain 2- to 2.5-fold more cholesteryl ester molecules than normals. ABL-HDL can be modified towards normal HDL by allowing VLDL triglycerides to exchange for ABL-HDL cholesteryl esters, followed by addition of lipoprotein lipase and hydrolysis of the triglycerides. In addition, ABL plasma contains a previously undescribed small and spherical (61 +/- 8 A) protein-rich (63% by weight) HDL fraction, which we call ABL-HDL4. Our data suggest that absence of cholesteryl ester transfer to triglyceride-rich lipoprotein in ABL causes accumulation of abnormally large cholesteryl ester-rich particles.
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PMID:Abnormal high density lipoproteins of abetalipoproteinemia: relevance to normal HDL metabolism. 716 57

The ubiquitous human POU domain protein, Oct-1, and the related B-cell protein, Oct-2, regulate transcription from a variety of eukaryotic genes by binding to a common cis-acting octamer element, 5'-ATTTGCAT-3'. The binding of Oct-1 and Oct-2 to the functionally important lipoprotein lipase (LPL) promoter octamer site was stimulated by the general transcription factor, TFIIB. Comparative analysis of the LPL, histone H2B (H2B), and herpes simplex virus ICPO gene promoter octamer sites revealed that nucleotide sequences within and flanking the octamer sequence determined the degree of TFIIB-mediated stimulation of Oct-1 DNA binding. TFIIB was found to decrease the rate of dissociation of Oct-1 from the LPL octamer site, whereas it increased the rate of association, as well as decreased the rate of dissociation, of Oct-1 from the H2B octamer site. A monoclonal antibody against TFIIB immunoprecipitated a ternary complex containing TFIIB, Oct-1, and the LPL and H2B octamer binding sites. TFIIB did not alter the DNase I footprints generated by Oct-1 on the LPL and H2B promoters. However, Oct-1 on the TATA-binding protein and TFIIB from footprinting the perfect TATA box sequence located 5' of the LPL, NF-Y binding site. In transfection experiments, transcription from the reporters containing the LPL octamer, and either the SV40 or the yeast transcription factor GAL4-dependent enhancers, initiated at a precise position within the octamer sequence. Transcription from reporters containing the H2B octamer and the SV40 enhancer initiated at several positions within and flanking the octamer site, whereas transcription initiated at a precise position within the octamer from reporters with both the H2B octamer and the GAL4-dependent enhancer. These results suggest that octamers and their flanking sequences play an important role in positioning the site of transcription initiation, and that this could be a function of the interaction of Oct-1 with TFIIB.
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PMID:Interaction of Oct-1 with TFIIB. Implications for a novel response elicited through the proximal octamer site of the lipoprotein lipase promoter. 764 49