HTS1/YPR033C Summary Help

HTS1 BASIC INFORMATION

Standard Name HTS1 1, 2, 3
Systematic Name YPR033C
Alias TSM4572
Feature Type ORF, Verified
Description Cytoplasmic and mitochondrial histidine tRNA synthetase; encoded by a single nuclear gene that specifies two messages; efficient mitochondrial localization requires both a presequence and an amino-terminal sequence (4, 5 and see Summary Paragraph)
Name Description Histidine-Trna Synthetase 5
Gene Product Alias histidyl-tRNA synthetase 5
GO Annotations All HTS1 GO evidence and references
    View Computational GO annotations for HTS1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Mutant Phenotype All HTS1 Phenotype details and references
Large-scale survey
null
Interactions HTS1 All interactions details and references
4 total interaction(s) for 4 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 3
  • Two-hybrid: 1
Sequence Information
ChrXVI:639016 to 637376 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Genetic position: 26 cM
Last Update Coordinates: 2004-07-21 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..1641 639016..637376 2004-07-21 1996-07-31
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000006237

HTS1 RESOURCES

Click on map for expanded view
SGD ORF mapGBrowse
SGD ORF map
 GBrowse
  • Literature
  • Retrieve Sequences
  • Sequence Analysis Tools
  • Protein Info & Structure
  • Localization Resources
  • Interactions
  • Phenotype Resources
  • Maps & Displays
  • Comparison Resources
  • Functional Analysis

Click on histogram for expression summary
Expression Summary histogram

ADDITIONAL INFORMATION for HTS1

SUMMARY PARAGRAPH for HTS1

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 (6, 7 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 (6, 7, 8 and references therein).

Last updated: 2008-07-14

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) 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
5) 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
6) Delarue M  (1995) Aminoacyl-tRNA synthetases. Curr Opin Struct Biol 5(1):48-55
7) Arnez JG and Moras D  (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem Sci 22(6):211-6
8) 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