Disease relevance of HIS7

• The ARO4 terminator and the HIS7 promoter regions are sensitive to Micrococcus nuclease (Mnase) and separated by a positioned nucleosome [1].
• Cys 77 was identified as the site of modification in the heterodimeric IGPS from Escherichia coli (HisHF) by tryptic digest and FABMS [2].

High impact information on HIS7

• Multiple factors prevent transcriptional interference at the yeast ARO4-HIS7 locus [3].
• The abolishment of the Abf1p-binding site within the HIS7 promoter significantly enhances transcriptional interference, resulting in a histidine auxotrophic strain [3].
• The open reading frames of ARO4 and HIS7 are tandemly transcribed and are separated by 416 bp [3].
• Under conditions of simultaneous amino acid starvation and adenine limitation the effects of GCN4p and BAS1/2p are additive and both factors are necessary for maximal HIS7 transcription [4].
• The HIS7 gene is activated by GCN4p under environmental conditions of amino acid starvation through two synergistic upstream sites GCRE1 and GCRE2 [4].

Biological context of HIS7

• The HSM3 gene maps to the right arm of chromosome II, 25 cM distal to the HIS7 gene [5].
• First, the N-terminal and C-terminal segments of the deduced HIS7 amino acid sequence show significant homology to prokaryotic monofunctional glutamine amidotransferases and cyclases, respectively, involved in histidine biosynthesis [6].
• HIS7 gene expression is regulated by the general control system of amino acid biosynthesis [6].
• According to the model that we propose, the bifunctional HIS7 gene is the outcome of a gene fusion event between two independent ancestral cistrons encoding an amidotransferase and a cyclase, respectively [7].
• The molecular evolution of the yeast HIS6 and HIS7 genes is also discussed [8].

Associations of HIS7 with chemical compounds

• The HIS7 gene of Saccharomyces cerevisiae encodes a bifunctional glutamine amidotransferase:cyclase catalyzing two reactions that lead to the formation of biosynthetic intermediates of the amino acid histidine and the purine adenine [4].
• Amino acid and adenine cross-pathway regulation act through the same 5'-TGACTC-3' motif in the yeast HIS7 promoter [4].
• One fluphenazine-resistance mutation, fsr1, was located near the his7 locus on chromosome II [9].
• The imidazole rings of the two key catalytic residues, His7 and His141, are not parallel as in the yeast phosphoglycerate mutase [10].

Regulatory relationships of HIS7

• The BAS1p-BAS2p complex activates the HIS7 gene in response to adenine limitation [4].
• An Arabidopsis cDNA encoding a bifunctional glutamine amidotransferase/cyclase suppresses the histidine auxotrophy of a Saccharomyces cerevisiae his7 mutant [11].

Other interactions of HIS7

• Tetrad analysis of crosses between rib5 and other markers on chromosome II shows that the RIB5 gene is located on the right arm of this chromosome, closely linked to HIS7 [12].
• DPB3 was mapped to chromosome II, 30 cM distal to his7 [13].
• Each of the his1-his7 mutant strains were unable to grow in the presence of elevated levels of Cu, Co, or Ni at nearly neutral pHs, in contrast to His(+) strains, which grew under these conditions [14].
• Regulation of the yeast HIS7 gene by the global transcription factor Abf1p [15].
• The locus of CAD2 was mapped by gene linkage to a site 15.5 centimorgans to the right of the his7 locus on the right arm of chromosome II [16].

Analytical, diagnostic and therapeutic context of HIS7

• The fused structural feature of the HIS7 protein and the development of a high-level production system for the active enzyme elevate the potential for determination of its three-dimensional structure through X-ray crystallography [17].

References