MSR1/YHR091C Summary Help

MSR1 BASIC INFORMATION

Standard Name MSR1 1
Systematic Name YHR091C
Feature Type ORF, Verified
Description Mitochondrial arginyl-tRNA synthetase (1 and see Summary Paragraph)
Name Description Mitochondrial tRNA Synthetase aRginine 1
Gene Product Alias mitochondrial arginyl-tRNA synthetase 1
GO Annotations All MSR1 GO evidence and references
    View Computational GO annotations for MSR1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Mutant Phenotype All MSR1 Phenotype details and references
Classical genetics
null
reduction of function
Large-scale survey
null
Interactions MSR1 All interactions details and references
  View additional details at BioGRID
6 total interaction(s) for 5 unique genes/features.
Physical Interactions
  • Two-hybrid: 1
Genetic Interactions
  • Synthetic Growth Defect: 2
  • Synthetic Lethality: 3
Sequence Information
ChrVIII:286772 to 284841 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Last Update Coordinates: 2005-11-07 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..1932 286772..284841 2005-11-07 1996-07-31
Post-translational Modifications PhosphoGRID | PhosphoPep Database
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000001133

MSR1 RESOURCES

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SGD ORF mapGBrowse
SGD ORF map
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  • Protein Info & Structure
  • Localization Resources
  • Interactions
  • Phenotype Resources
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  • Functional Analysis

Click on histogram for expression summary
Expression Summary histogram

ADDITIONAL INFORMATION for MSR1

SUMMARY PARAGRAPH for MSR1

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 (2, 3 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 (2, 3, 4 and references therein).

Last updated: 2008-07-14

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for MSR1]

1) Tzagoloff A and Shtanko A  (1995) Mitochondrial and cytoplasmic isoleucyl-, glutamyl- and arginyl-tRNA synthetases of yeast are encoded by separate genes. Eur J Biochem 230(2):582-6
2) Delarue M  (1995) Aminoacyl-tRNA synthetases. Curr Opin Struct Biol 5(1):48-55
3) Arnez JG and Moras D  (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem Sci 22(6):211-6
4) 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