HTS1/YPR033C Summary Help

Standard Name HTS1 1, 2, 3
Systematic Name YPR033C
Alias TSM4572 4 , TS4572 5
Feature Type ORF, Verified
Description Cytoplasmic and mitochondrial histidine tRNA synthetase; efficient mitochondrial localization requires both a presequence and an amino-terminal sequence; mutations in human ortholog HARS2 are associated with Perrault syndrome (6, 7, 8 and see Summary Paragraph)
Name Description Histidine-Trna Synthetase 7
Gene Product Alias histidyl-tRNA synthetase 7
Chromosomal Location
ChrXVI:639019 to 637379 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Genetic position: 26 cM
Gene Ontology Annotations All HTS1 GO evidence and references
  View Computational GO annotations for HTS1
Molecular Function
Manually curated
High-throughput
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 7 genes
Resources
Large-scale survey
null
reduction of function
Resources
31 total interaction(s) for 27 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 9
  • Affinity Capture-RNA: 1
  • Two-hybrid: 1

Genetic Interactions
  • Dosage Rescue: 1
  • Negative Genetic: 9
  • Positive Genetic: 9
  • Synthetic Lethality: 1

Resources
Expression Summary
histogram
Resources
Length (a.a.) 546
Molecular Weight (Da) 59,952
Isoelectric Point (pI) 7.76
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrXVI:639019 to 637379 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Genetic position: 26 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1641 639019..637379 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 | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000006237
SUMMARY PARAGRAPH for HTS1

About aminoacyl-tRNA synthetases...

In a process critical for accurate translation of the genetic code, aminoacyl-tRNA synthetases (aka aminoacyl-tRNA ligases) attach amino acids specifically to cognate tRNAs, thereby "charging" the tRNAs. The catalysis is accomplished via a two-step mechanism. First, the synthetase activates the amino acid in an ATP-dependent reaction, producing aminoacyl-adenylate and releasing inorganic pyrophosphate (PPi). Second, the enzyme binds the correct tRNA and transfers the activated amino acid to either the 2' or 3' terminal hydroxyl group of the tRNA, forming the aminoacyl-tRNA and AMP (9, 10 and references therein).

Aminoacyl-tRNA synthetases possess precise substrate specificity and, despite their similarity in function, vary in size, primary sequence and subunit composition. Individual members of the aminoacyl-tRNA synthetase family can be categorized in one of two classes, depending on amino acid specificity. Class I enzymes (those specific for Glu, Gln, Arg, Cys, Met, Val, Ile, Leu, Tyr and Trp) typically contain two highly conserved sequence motifs, are monomeric or dimeric, and aminoacylate at the 2' terminal hydroxyl of the appropriate tRNA. Class II enzymes (those specific for Gly, Ala, Pro, Ser, Thr, His, Asp, Asn, Lys and Phe) typically contain three highly conserved sequence motifs, are dimeric or tetrameric, and aminoacylate at the 3' terminal hydroxyl of the appropriate tRNA (9, 10, 11 and references therein).

Last updated: 2008-07-14 Contact SGD

References cited on this page View Complete Literature Guide for HTS1
1) Sandbaken, M. and Culbertson, M.  (1989) Personal Communication, Mortimer Map Edition 10
2) Toyn, J. and Johnston, L.  (1992) Personal Communication, Mortimer Map Edition 11
3) Natsoulis, G., et al.  (1989) ; Personal Communication, Mortimer Map Edition 10
4) Hilger F, et al.  (1982) Genetic mapping of arg, cpa, car and tsm genes in Saccharomyces cerevisiae by trisomic analysis. Curr Genet 6(2):93-8
5) Messenguy F and Scherens B  (1990) Induction of "General Control" and thermotolerance in cdc mutants of Saccharomyces cerevisiae. Mol Gen Genet 224(2):257-63
6) Chiu MI, et al.  (1992) HTS1 encodes both the cytoplasmic and mitochondrial histidyl-tRNA synthetase of Saccharomyces cerevisiae: mutations alter the specificity of compartmentation. Genetics 132(4):987-1001
7) Natsoulis G, et al.  (1986) The HTS1 gene encodes both the cytoplasmic and mitochondrial histidine tRNA synthetases of S. cerevisiae. Cell 46(2):235-43
8) Pierce SB, et al.  (2011) Mutations in mitochondrial histidyl tRNA synthetase HARS2 cause ovarian dysgenesis and sensorineural hearing loss of Perrault syndrome. Proc Natl Acad Sci U S A 108(16):6543-8
9) Delarue M  (1995) Aminoacyl-tRNA synthetases. Curr Opin Struct Biol 5(1):48-55
10) Arnez JG and Moras D  (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem Sci 22(6):211-6
11) Eriani G, et al.  (1990) Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature 347(6289):203-6