Disease relevance of HIS5

• The deduced amino acid sequence was compared to the Saccharomyces cerevisiae HIS5, Escherichia coli HisC, and Salmonella typhimurium HisC proteins, all of which are imidazole acetol phosphate transaminases [1].
• A search of the DNA and protein data bases revealed that this open reading frame encodes histidinol-phosphate aminotransferase (EC 2.6.1.9), the sequence of which is also known for E. coli, Bacillus subtilis, and Saccharomyces cerevisiae [2].

High impact information on HIS5

• The residues involved in the E-box recognition are His5, Glu9 and Arg13, as already reported for bHLH/Zip proteins MAX and USF, and are different from those recognized by bHLH proteins MyoD and E47, although PHO4 is a bHLH protein [3].
• These vectors carry ADE2 or HIS5 as the selectable marker, enabling direct use in AB1380, the host strain of most publicly available YAC libraries [4].
• Leaky expression was eliminated using 3-aminotriazole and gene conversion was eliminated by using the Schizosaccharomyces pombe his5+ gene, resulting in a 5- to 10-fold improvement in the efficiency of SGA [5].
• We have constructed a new telomere truncation vector, pGR8, which incorporates two selectable markers, HIS5 and LYS2 [6].
• That the DNA fragment contains the yeast HIS5 gene was confirmed by the integration of the cloned plasmid into the his5 region of the yeast chromosome [7].

Chemical compound and disease context of HIS5

• The cloned yeast HIS5 gene weakly complemented the E. coli hisC mutation and gave rise to a slow-growing E. coli transformant without addition of histidine [7].

Biological context of HIS5

• The REV7 gene is located about 12 cM distal to HIS5 on chromosome IX [8].
• The nucleotide sequence of a 2.1 kb DNA fragment bearing the HIS5 gene of Saccharomyces cerevisiae, which encodes histidinol-phosphate aminotransferase (EC 2.6.1.9), has been determined [9].
• Histidine auxotrophs of wild-type strain I-182 of Candida oleophila, produced using ethyl methanesulfonate, were transformed with plasmids containing the HIS3, HIS4 and HIS5 genes of Saccharomyces cerevisiae [10].
• A yeast DNA fragment complementing a yeast his5 mutation was cloned on a shuttle vector, YRp7, by transformation of the yeast host with plasmid DNA prepared from a gene bank constructed in the Escherichia coli host [7].
• An improved host-vector system for Candida maltosa using a gene isolated from its genome that complements the his5 mutation of Saccharomyces cerevisiae [11].

Associations of HIS5 with chemical compounds

• Histidine auxotrophy was complemented by the HIS5 gene of S. cerevisiae [10].
• The OGD1 gene, affecting 2-oxoglutarate dehydrogenase in S. cerevisiae, is closely linked to HIS5 on chromosome IX [12].

Regulatory relationships of HIS5

• The rho- mutation also increased the expression of the PHO5 gene under the control of the HIS5 promoter in a plasmid and the ACT1 gene in the yeast chromosome, but did not increase the expression of the ribosomal RNA gene [13].

Other interactions of HIS5

• The HIS5 and PHO5 genes at their original chromosomal positions were, however, not affected by the bel2 mutation [14].
• The consensus sequence closest to the open reading frame was shown to be necessary but not sufficient for general amino acid control, by examination of beta-galactosidase appearance in S. cerevisiae cells carrying various mutant HIS5 promoter regions fused to the lac'Z gene and inserted at the leu2 locus of chromosome III [9].
• Tetrad analysis placed the UVS112 gene on the left arm of chromosome IX, approximately 20 cM from HIS5 [15].
• This enzyme is encoded by the HIS3 gene in S. cerevisiae and the his5+ gene in S. pombe [16].
• The SGA1 sporulation-specific, intracellular glucoamylase-encoding gene is located on the left arm of chromosome IX, 32 kb proximal of HIS5 [17].

References