Disease relevance of HIS6

• The HIS6 gene from Saccharomyces cerevisiae strain YNN282 is able to complement both the S. cerevisiae his6 and the Escherichia coli hisA mutations [1].
• Finally, baculoviruses encoding a His6-tagged metaxin 2 and an untagged metaxin 1 lacking its C-terminal transmembrane domain were produced and used separately or in combination to infect Sf21 insect cells [2].

High impact information on HIS6

• MIF2 is a unique sequence located 15 cM distal to HIS6 on chromosome IX that induces a high frequency of chromosome VII loss and a lower frequency of chromosome V loss when present in high copy number; it has no effect on mitotic recombination [3].
• The His6-tagged Sec7 domain from ySec7p (rySec7d) synthesized in Escherichia coli enhanced binding of guanosine 5'-[gamma-[35S]thio]triphosphate by recombinant yeast ARF1 (ryARF1) and ryARF2 but not by ryARF3 [4].
• RPB3 was found to be an essential single-copy gene that is tightly linked to HIS6 on chromosome IX [5].
• The sst1 gene was mapped to within 6.9 centimorgans of his6 on chromosome IX [6].
• His6-tagged Tsc10p was expressed in Escherichia coli and isolated by nickel-nitrilotriacetic acid column chromatography [7].

Biological context of HIS6

• The molecular evolution of the yeast HIS6 and HIS7 genes is also discussed [1].
• Fusion proteins produced from YGALSET plasmids include a leader peptide at the N terminus that encodes both a T7 gene 10 epitope tag and a His6 affinity tag [8].
• Complete DNA sequences encoding the Arabidopsis thaliana STP1 monosaccharide/H+ symporter or a histidine-tagged STP1-His6 protein were expressed in baker's yeast Saccharomyces cerevisiae [9].
• The suppressor genes were mapped on the left arm of chromosome I proximal to the his6 gene [10].
• Fluorescence resonance energy transfer experiments showed that n-dodecyl-beta-D-maltoside-solubilized UCP1-His6 retained its PN (purine nucleotide)-binding capacity [11].

Anatomical context of HIS6

• A V5 epitope and His6-tagged version of Ynl275wp was expressed in yeast and was localized to the plasma membrane by subcellular fractionation and immunofluorescence labeling [12].
• In comparison N-glycosylated hisGal-T transiently expressed in COS cells was secreted as a soluble active enzyme and could be purified in one single step by virtue of the His6-tag [13].
• One library was derived from mice immunized with recombinant CDC2aAt N-terminally fused to a His6-tag (His-CDC2aAt) and the other was made out of an anti-PSTAIRE hybridoma cell line [14].

Associations of HIS6 with chemical compounds

• Paralogous histidine biosynthetic genes: evolutionary analysis of the Saccharomyces cerevisiae HIS6 and HIS7 genes [1].
• STP1-His6 protein is functionally active after solubilization with octyl-beta-D-glucoside, which was shown by insertion of the protein into proteoliposomes by detergent dilution and determination of the resulting transport capacity [9].
• The intrinsic fluorescence of two CCP derivatives with the quencher pentaammineruthenium(III) covalently attached to His6 and His60 has also been characterized [15].
• A genetically modified (His6-tagged) form of the mitochondrial F1-ATPase (MW = 370 kDa) has been purified from the yeast Saccharomyces cerevisiae and crystallized in the presence of polyethelene glycol (PEG) 6000 as a precipitant, 1 mM NiCl2, 1 mM Mg AMP-PNP and 50 microM Mg ADP [16].

Regulatory relationships of HIS6

• Recombinant Trr1 was expressed in Escherichia coli as a His6-tagged fusion protein and purified by nickel-affinity chromatography [17].

Analytical, diagnostic and therapeutic context of HIS6

• Plc1p, modified by in-frame insertion of a His6 tract and a c-myc epitope near its amino terminus, was overexpressed from the GAL1 promoter, partially purified by nickel chelate affinity chromatography, and shown to be an active PLC enzyme in vitro with properties similar to those of its mammalian counterparts [18].
• This protein-protein interaction has been validated by immunoprecipitation in both COS-1 and Huh7 cells and by His6 pull-down assays [19].
• X-ray crystallography showed that a5Ru is coordinated to His60 in one derivative [Fox et al. (1990) J. Am. Chem. Soc. 112, 7426]; HPLC and mass spectral analysis of the tryptic peptides of the other derivative identified a peptide (MW = 1469 Da) corresponding to residues 1-12 of CCP plus a5Ru, indicating His6 as the site of modification [20].

References