TRP5/YGL026C Summary Help

Standard Name TRP5 1, 2
Systematic Name YGL026C
Feature Type ORF, Verified
Description Tryptophan synthase, catalyzes the last step of tryptophan biosynthesis; regulated by the general control system of amino acid biosynthesis (3, 4 and see Summary Paragraph)
Name Description TRyPtophan requiring
Chromosomal Location
ChrVII:448535 to 446412 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Genetic position: -22 cM
Gene Ontology Annotations All TRP5 GO evidence and references
  View Computational GO annotations for TRP5
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
High-throughput
Pathways
Mutant phenotypes All TRP5 Phenotype evidence and references
Classical genetics
null
unspecified
Large-scale survey
null
Resources
interactions All TRP5 Interaction evidence and references
23 total interaction(s) for 19 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 19
  • Two-hybrid: 3
Genetic Interactions
  • Synthetic Rescue: 1
Resources
Expression Summary
histogram
Resources
Protein Information All TRP5 Protein evidence and references
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrVII:448535 to 446412 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Genetic position: -22 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..2124 448535..446412 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 SGDIDS000002994
SUMMARY PARAGRAPH for TRP5

TRP5 encodes tryptophan synthase, which catalyzes the last reaction of tryptophan biosynthesis, cleaving indole-3-phosphate to yield an indole group which is then condensed with serine to form tryptophan (5, 6; reviewed in 7). The two steps of this reaction are mediated by two different active sites in Trp5p; in most other organisms, these two active sites are carried on separate proteins, for example, TrpA and TrpB in E. coli (3, 8, 7). Trp5p is active as a dimer (9). Null mutations in trp5 confer tryptophan auxotrophy, as well as sensitivity to phenethyl alcohol (10) and resistance to 5-fluoroanthranilic acid (11).

Like many genes encoding amino acid biosynthetic enzymes, TRP5 is subject to the general control of amino acid biosynthesis (reviewed in 12). Under conditions of amino acid limitation, transcription of TRP5 and other genes is activated via the Gcn4p transcriptional activator (13, 14, 4). The TRP5 promoter contains two binding sites for Gcn4p (4).

Last updated: 2009-07-14

References cited on this page View Complete Literature Guide for TRP5
1) Balzi, E.  (1989) Personal Communication, Mortimer Map Edition 10
2) Plotkin, D.J.  (1978) Commitment to meiotic recombination: a temporal analysis. Ph.D Thesis
3) Zalkin H and Yanofsky C  (1982) Yeast gene TRP5: structure, function, regulation. J Biol Chem 257(3):1491-500
4) Moye WS and Zalkin H  (1985) Deletion mapping the yeast TRP5 control region. J Biol Chem 260(8):4718-23
5) Bailey CJ and Turner PD  (1983) Purification and properties of tryptophan synthase from baker's yeast (Saccharomyces cerevisiae). Biochem J 209(1):151-7
6) Bartholmes P, et al.  (1979) Purification of tryptophan synthase from Saccharomyces cerevisiae and partial activity of its nicked subunits. Eur J Biochem 102(1):167-72
7) Braus GH  (1991) Aromatic amino acid biosynthesis in the yeast Saccharomyces cerevisiae: a model system for the regulation of a eukaryotic biosynthetic pathway. Microbiol Rev 55(3):349-70
8) Crawford IP, et al.  (1987) Crucial role of the connecting region joining the two functional domains of yeast tryptophan synthetase. J Biol Chem 262(1):239-44
9) Dettwiler M and Kirschner K  (1979) Tryptophan synthase from Saccharomyces cerevisiae is a dimer of two polypeptide chains of Mr 76000 each. Eur J Biochem 102(1):159-65
10) Meade JH and Manney TR  (1983) Sensitivity of tryptophan, tyrosine and phenylalanine mutants of Saccharomyces cerevisiae to phenethyl alcohol. Genetics 104(2):235-40
11) Toyn JH, et al.  (2000) A counterselection for the tryptophan pathway in yeast: 5-fluoroanthranilic acid resistance. Yeast 16(6):553-60
12) Hinnebusch AG  (2005) Translational regulation of gcn4 and the general amino Acid control of yeast *. Annu Rev Microbiol 59:407-50
13) Delforge J, et al.  (1975) The regulation of arginine biosynthesis in Saccharomyces cerevisiae. The specificity of argR- mutations and the general control of amino-acid biosynthesis. Eur J Biochem 57(1):231-9
14) Kinney DM and Lusty CJ  (1989) Arginine restriction induced by delta-N-(phosphonacetyl)-L-ornithine signals increased expression of HIS3, TRP5, CPA1, and CPA2 in Saccharomyces cerevisiae. Mol Cell Biol 9(11):4882-8