MSM1/YGR171C Summary Help

Standard Name MSM1 1
Systematic Name YGR171C
Feature Type ORF, Verified
Description Mitochondrial methionyl-tRNA synthetase (MetRS); functions as a monomer in mitochondrial protein synthesis; functions similarly to cytoplasmic MetRS although the cytoplasmic form contains a zinc-binding domain not found in Msm1p (1, 2, 3 and see Summary Paragraph)
Name Description Mitochondrial aminoacyl-tRNA Synthetase, Methionine 1
Gene Product Alias mitochondrial methionyl-tRNA synthetase 1
Chromosomal Location
ChrVII:842551 to 840824 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Gene Ontology Annotations All MSM1 GO evidence and references
  View Computational GO annotations for MSM1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Regulators 3 genes
Resources
Classical genetics
null
Large-scale survey
null
unspecified
Resources
47 total interaction(s) for 47 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 1
  • Affinity Capture-RNA: 2
  • Reconstituted Complex: 1

Genetic Interactions
  • Dosage Lethality: 1
  • Negative Genetic: 24
  • Positive Genetic: 16
  • Synthetic Growth Defect: 1
  • Synthetic Rescue: 1

Resources
Expression Summary
histogram
Resources
Length (a.a.) 575
Molecular Weight (Da) 66,734
Isoelectric Point (pI) 9.27
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrVII:842551 to 840824 | 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..1728 842551..840824 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 SGDIDS000003403
SUMMARY PARAGRAPH for MSM1

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 MSM1
1) Tzagoloff A, et al.  (1989) Characterization of MSM1, the structural gene for yeast mitochondrial methionyl-tRNA synthetase. Eur J Biochem 179(2):365-71
2) Schwob E, et al.  (1988) Purification of the yeast mitochondrial methionyl-tRNA synthetase. Common and distinctive features of the cytoplasmic and mitochondrial isoenzymes. Eur J Biochem 178(1):235-42
3) Senger B, et al.  (2001) Yeast cytoplasmic and mitochondrial methionyl-tRNA synthetases: two structural frameworks for identical functions. J Mol Biol 311(1):205-16
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