Disease relevance of Gtf2h4

• Using reverse transcription-PCR targeting of the p44 genes of the agent of human granulocytic ehrlichiosis (HGE) with primers flanking the hypervariable region, we show differential expression in a murine model of HGE infection and during tick transmission [1].
• Similarly, the p44 genes were differentially expressed in infected C3H mice, in SCID mice, and in cultured HGE bacteria [1].
• In addition to the viral envelope-related proteins (gPr85, gp70, and gp52) detected by precipitation with goat anti-Rauscher gp70 antiserum from tumor cell lines induced by parental Friend virus strains, BSB-induced cell lines also expressed gp80, p52, and gp45 products precipitable with the same antiserum [2].

High impact information on Gtf2h4

• However, additional amino acid substitutions for phenylalanine 429 demonstrated a strong correlation between activation of the dhfr promoter and binding of CBP, but not TFIIH or TBP [3].
• Phosphorylation of p52 was also on threonine residues [4].
• Phosphamino acid analysis showed that phosphorylation of p90 and p52 occurred mainly on serine residues [4].
• The conversion of p52 to GP85 requires further glycosylation (both complex type N-linked and O-linked) which takes place in the Golgi complex within 10-20 min after p52 is synthesized [5].
• Using a standard pulse-chase protocol, we have detected a 52-kDa polypeptide precursor (p52) within the first 5 min of pulse labeling which contains a high mannose-type N-linked oligosaccharide chains [5].

Biological context of Gtf2h4

• DNA sequence analysis identified this gene as the mouse homologue of the human gene encoding the p52 subunit of the TFIIH transcription/DNA repair factor [6].
• Sequence analysis of p52 cDNA from congenic mouse strains detected an amino acid polymorphism at position 209, which results in the substitution of a threonine in the H2b haplotype to a methionine in the H2a,d haplotypes [6].
• Moreover, the fact that phosphorylation of p52 was specific to phorbol ester activation may suggest its involvement in tumor promotion [4].
• Thus, differential p44 expression exists in vivo and in vitro and could provide a basis for antigenic variation [1].

Anatomical context of Gtf2h4

• The p44 genes were differentially expressed in salivary glands of infected nymphal ticks removed during transmission feeding but not in nonfeeding infected ticks [1].

Associations of Gtf2h4 with chemical compounds

• Proteins of Mr 34, 38, 40, and 44 (p34 ... p44) were strongly phosphorylated on tyrosine residues in freshly prepared sperm samples and at the same level during all subsequent treatments [7].

References