MSR1/YHR091C Summary Help

Standard Name MSR1 1
Systematic Name YHR091C
Feature Type ORF, Verified
Description Mitochondrial arginyl-tRNA synthetase; mutations in human ortholog are associated with pontocerebellar hypoplasia type 6; MSR1 has a paralog, YDR341C, that arose from the whole genome duplication (1, 2, 3 and see Summary Paragraph)
Name Description Mitochondrial tRNA Synthetase aRginine 1
Gene Product Alias mitochondrial arginyl-tRNA synthetase 1
Chromosomal Location
ChrVIII:286770 to 284839 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Gene Ontology 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
Regulators 3 genes
Resources
Classical genetics
null
reduction of function
Large-scale survey
null
unspecified
Resources
9 total interaction(s) for 8 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 2
  • Two-hybrid: 1

Genetic Interactions
  • Synthetic Growth Defect: 2
  • Synthetic Lethality: 3
  • Synthetic Rescue: 1

Resources
Expression Summary
histogram
Resources
Length (a.a.) 643
Molecular Weight (Da) 73,693
Isoelectric Point (pI) 10.19
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrVIII:286770 to 284839 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1932 286770..284839 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 SGDIDS000001133
SUMMARY PARAGRAPH for MSR1

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 (4, 5 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 (4, 5, 6 and references therein).

Last updated: 2008-07-14 Contact SGD

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) Byrne KP and Wolfe KH  (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
3) Cassandrini D, et al.  (2013) Pontocerebellar hypoplasia type 6 caused by mutations in RARS2: definition of the clinical spectrum and molecular findings in five patients. J Inherit Metab Dis 36(1):43-53
4) Delarue M  (1995) Aminoacyl-tRNA synthetases. Curr Opin Struct Biol 5(1):48-55
5) Arnez JG and Moras D  (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem Sci 22(6):211-6
6) 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