Disease relevance of Tcea1

• RNA blot analysis demonstrated the presence of four species of mRNA that hybridized with S-II cDNA in Ehrlich ascites tumor cells [1].
• The recombinant SII-K1 produced in Escherichia coli stimulated RNA polymerase II as did general S-II [2].

High impact information on Tcea1

• We further provide evidence for motifs (S-N and S-II) at the NH2 and COOH terminus of bcl-2, which are crucial for its activity [3].
• Transcription elongation factor S-II is required for definitive hematopoiesis [4].
• S-II(-/-) embryos had a decreased number of definitive erythrocytes in the peripheral blood and disturbed erythroblast differentiation in fetal liver [4].
• The presence of phenotypically defined hematopoietic stem cells and in vitro colony-forming hematopoietic progenitors in S-II(-/-) fetal liver indicates that S-II is dispensable for the generation and differentiation of hematopoietic stem cells [4].
• There was a dramatic increase in apoptotic cells in S-II(-/-) fetal liver, which was consistent with a reduction in Bcl-x(L) gene expression [4].

Chemical compound and disease context of Tcea1

• (3) S-II' was phosphorylated more than S-II when Ehrlich ascites tumor cells were labeled in vivo with [32P]orthophosphate [5].

Biological context of Tcea1

• Linkage analysis showed that Tcea1 and Tcea1-ps1 are mapped on mouse chromosomes 1 and 15, respectively [6].
• We also identified a processed pseudogene (Tcea1-ps1) with a sequence highly homologous to those of S-II cDNAs but containing a translation termination codon within its open reading frame [6].
• Recent studies suggest that S-II participates in gene-specific transcriptional activation in vivo, despite the fact that it directly binds RNA polymerase II and does not recognize specific DNA sequences [7].
• The primary structure of S-II was determined by nucleotide sequence analysis of these clones [1].
• During mouse embryonic development, no significant expression of the SII-K1 gene was detected before the formation of these tissues [2].

Anatomical context of Tcea1

• S-II-deficient fetal liver cells, however, exhibited a loss of long-term repopulating potential when transplanted into lethally irradiated adult mice, indicating that S-II deficiency causes an intrinsic defect in the self-renewal of hematopoietic stem cells [4].
• SII-T1 is a tissue-specific member of the transcription elongation factor S-II that is expressed specifically in male germ cells [8].
• The gene for SII-K1 was found to be expressed strongly in the heart, liver, skeletal muscle and kidney, but not in other tissues examined [2].
• We investigated the expression profile of tissue-specific S-II during development using an isolated cDNA, termed mouse S-II-T1, whose transcripts are detected almost exclusively in testis [9].
• SII was purified from calf thymus tissue to apparent homogeneity by a rapid procedure [10].

Associations of Tcea1 with chemical compounds

• Manganese prevented accurate transcription, but it was essential for expression of the stimulatory activity of S-II [11].
• From analysis of the amino acid compositions and tryptic peptide maps of these proteins labeled with radioiodinated Bolton-Hunter reagent, it was concluded that S-I(b) is a part of S-II located at either the amino- or carboxyl-terminal and that only this region mainly contains radioiodinatable amino acid residues when labeled using 125I [12].
• To identify the molecular region of S-II that defines species specificity, we constructed six hybrid S-II molecules consisting of three regions from yeast and/or Ehrlich cell S-II and examined their activity in terms of RNA polymerase II specificity and suppression of 6-azauracil sensitivity in the yeast S-II null mutant [13].
• The comparison of amino acid sequences suggests that DmSII is comprised of two domains homologous to mouse SII separated by a flexible, serine rich region of low homology [14].
• Neither of these inhibitors, 5, 6-dichloro-1-beta-D-ribofuranosylbenzimidazole (DRB) and actinomycin D, affected the phosphorylation of S-II under conditions where 75 to 98% of RNA synthesis was inhibited at the initiation and elongation step, respectively [15].

Physical interactions of Tcea1

• Identification of a novel tissue-specific transcriptional activator FESTA as a protein that interacts with the transcription elongation factor S-II [7].

Regulatory relationships of Tcea1

• Furthermore, deletion of the C-terminal tail of FESTA dramatically reduced its trans-activating ability and abolished its interaction with S-II [7].

Other interactions of Tcea1

• FESTA is expressed specifically in kidney and spleen, supporting our notion that S-II participates in gene-specific regulation [7].

Analytical, diagnostic and therapeutic context of Tcea1

• Molecular cloning and characterization of cDNA for eukaryotic transcription factor S-II [1].
• Neither caloric restriction nor age had an effect on the level of mRNA for insulin-like growth factor-I, RNA polymerase II elongation-factor S-II, or transcription factors Sp1, CCAAT and enhancer binding protein, or proto-oncogene c-jun [16].

References