CDC60/YPL160W Summary Help

Standard Name CDC60 1
Systematic Name YPL160W
Feature Type ORF, Verified
Description Cytosolic leucyl tRNA synthetase; ligates leucine to the appropriate tRNA (2 and see Summary Paragraph)
Also known as: LeuRS 2
Name Description Cell Division Cycle
Chromosomal Location
ChrXVI:246990 to 250262 | ORF Map | GBrowse
Genetic position: -65 cM
Gene Ontology Annotations All CDC60 GO evidence and references
  View Computational GO annotations for CDC60
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 4 genes
Classical genetics
gain of function
reduction of function
Large-scale survey
reduction of function
63 total interaction(s) for 53 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 24
  • Affinity Capture-RNA: 4
  • Affinity Capture-Western: 1
  • Two-hybrid: 3

Genetic Interactions
  • Negative Genetic: 31

Expression Summary
Length (a.a.) 1,090
Molecular Weight (Da) 124,140
Isoelectric Point (pI) 5.68
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXVI:246990 to 250262 | ORF Map | GBrowse
Genetic position: -65 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..3273 246990..250262 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000006081

CDC60 was first identified as a temperature sensitive mutant that arrested at START upon shift to the restrictive temperature (1). It encodes the cytoplasmic leucyl-tRNA synthase (2). The cell cycle arrest of the mutant is probably due to the block in protein synthesis that results from a lack of charged leucyl-tRNA (2). CDC60 is 50% identical to the Neurospora crassa cytosolic leucyl-tRNA synthase, and has regions of 19-21% identity to E. coli leucyl-, isoleucyl-, and methionyl-tRNA synthase (2). The yeast Cdc60p can aminoacylate E.coli tRNA-Leu (3).

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: 1999-09-01 Contact SGD

References cited on this page View Complete Literature Guide for CDC60
1) Bedard DP, et al.  (1981) New mutations in the yeast Saccharomyces cerevisiae affecting completion of "start". Curr Genet 4(3):205-14
2) Hohmann S and Thevelein JM  (1992) The cell division cycle gene CDC60 encodes cytosolic leucyl-tRNA synthetase in Saccharomyces cerevisiae. Gene 120(1):43-9
3) Soma A and Himeno H  (1998) Cross-species aminoacylation of tRNA with a long variable arm between Escherichia coli and Saccharomyces cerevisiae. Nucleic Acids Res 26(19):4374-81
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