HIS3/YOR202W Summary Help

Standard Name HIS3 1
Systematic Name YOR202W
Alias HIS10 2 , HIS8 2
Feature Type ORF, Verified
Description Imidazoleglycerol-phosphate dehydratase; catalyzes the sixth step in histidine biosynthesis; mutations cause histidine auxotrophy and sensitivity to Cu, Co, and Ni salts; transcription is regulated by general amino acid control via Gcn4p (1, 2, 3, 4, 5 and see Summary Paragraph)
Name Description HIStidine 1
Chromosomal Location
ChrXV:721946 to 722608 | ORF Map | GBrowse
Gbrowse
Genetic position: 112 cM
Gene Ontology Annotations All HIS3 GO evidence and references
  View Computational GO annotations for HIS3
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 3 genes
Resources
Pathways
Classical genetics
null
unspecified
Large-scale survey
null
Resources
40 total interaction(s) for 40 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 8
  • Affinity Capture-RNA: 4
  • Two-hybrid: 1

Genetic Interactions
  • Dosage Rescue: 3
  • Negative Genetic: 1
  • Phenotypic Enhancement: 10
  • Phenotypic Suppression: 12
  • Synthetic Lethality: 1

Resources
Expression Summary
histogram
Resources
Length (a.a.) 220
Molecular Weight (Da) 23,833
Isoelectric Point (pI) 6.37
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrXV:721946 to 722608 | ORF Map | GBrowse
SGD ORF map
Genetic position: 112 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..663 721946..722608 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000005728
SUMMARY PARAGRAPH for HIS3

HIS3 encodes imidazoleglycerol-phosphate dehydratase, which catalyzes the sixth step in histidine biosynthesis (5). The biosynthesis of histidine has been most extensively studied in Salmonella typhimurium and E. coli. The reactions and enzymes involved in histidine biosynthesis have been identified in many organisms, and are thoroughly reviewed in Alifano et al. (5). Mutations in HIS3, as well as in genes encoding other histidine biosynthetic enzymes, cause histidine auxotrophy and sensitivity to copper, cobalt, and nickel salts (4). Transcription of HIS3 is regulated by general amino acid control, in which the transcription factor Gcn4p plays a key role (reviewed in 6). HIS3 has been widely used in studies of transcriptional regulation (6) and as a selectable marker for plasmid constructs (for example, see 7 and 8).

Last updated: 1999-11-10 Contact SGD

References cited on this page View Complete Literature Guide for HIS3
1) Struhl K and Davis RW  (1977) Production of a functional eukaryotic enzyme in Escherichia coli: cloning and expression of the yeast structural gene for imidazole-glycerolphosphate dehydratase (his3). Proc Natl Acad Sci U S A 74(12):5255-9
2) Fink GR  (1964) GENE-ENZYME RELATIONS IN HISTIDINE BIOSYNTHESIS IN YEAST. Science 146(3643):525-7
3) Hope IA and Struhl K  (1985) GCN4 protein, synthesized in vitro, binds HIS3 regulatory sequences: implications for general control of amino acid biosynthetic genes in yeast. Cell 43(1):177-88
4) Pearce DA and Sherman F  (1999) Toxicity of copper, cobalt, and nickel salts is dependent on histidine metabolism in the yeast Saccharomyces cerevisiae. J Bacteriol 181(16):4774-9
5) Alifano P, et al.  (1996) Histidine biosynthetic pathway and genes: structure, regulation, and evolution. Microbiol Rev 60(1):44-69
6) Hinnebusch A  (1992) "General and Pathway-specific Regulatory Mechanisms Controlling the Synthesis of Amino Acid Biosynthetic Enzymes in Saccharomyces cerevisiae". Pp. 319-414 in The Molecular and Cellular Biology of the Yeast Saccharomyces: Gene Expression, edited by Jones EW, Pringle JR and Broach JR. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
7) Baganz F, et al.  (1997) Suitability of replacement markers for functional analysis studies in Saccharomyces cerevisiae. Yeast 13(16):1563-73
8) Sikorski RS and Hieter P  (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122(1):19-27