AIM10/YER087W Summary Help

Standard Name AIM10 1
Systematic Name YER087W
Feature Type ORF, Verified
Description Protein with similarity to tRNA synthetases; non-tagged protein is detected in purified mitochondria; null mutant is viable and displays elevated frequency of mitochondrial genome loss (1, 2, 3, 4 and see Summary Paragraph)
Name Description Altered Inheritance rate of Mitochondria 1
Chromosomal Location
ChrV:330576 to 332306 | ORF Map | GBrowse
Gbrowse
Gene Ontology Annotations All AIM10 GO evidence and references
  View Computational GO annotations for AIM10
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
High-throughput
Regulators 1 genes
Resources
Large-scale survey
null
unspecified
Resources
30 total interaction(s) for 30 unique genes/features.
Physical Interactions
  • Reconstituted Complex: 5

Genetic Interactions
  • Synthetic Growth Defect: 17
  • Synthetic Lethality: 8

Resources
Expression Summary
histogram
Resources
Length (a.a.) 576
Molecular Weight (Da) 65,880
Isoelectric Point (pI) 7.36
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrV:330576 to 332306 | ORF Map | GBrowse
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..1731 330576..332306 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 SGDIDS000000889
SUMMARY PARAGRAPH for AIM10

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 (5, 6 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 (5, 6, 7 and references therein).

Last updated: 2008-07-14 Contact SGD

References cited on this page View Complete Literature Guide for AIM10
1) Hess DC, et al.  (2009) Computationally driven, quantitative experiments discover genes required for mitochondrial biogenesis. PLoS Genet 5(3):e1000407
2) Sentandreu M, et al.  (1997) Isolation of a putative prolyl-tRNA synthetase (CaPRS) gene from Candida albicans. Yeast 13(14):1375-81
3) Giaever G, et al.  (2002) Functional profiling of the Saccharomyces cerevisiae genome. Nature 418(6896):387-91
4) Reinders J, et al.  (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J Proteome Res 5(7):1543-54
5) Delarue M  (1995) Aminoacyl-tRNA synthetases. Curr Opin Struct Biol 5(1):48-55
6) Arnez JG and Moras D  (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem Sci 22(6):211-6
7) 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