CCA1/YER168C Summary Help

Standard Name CCA1
Systematic Name YER168C
Alias TNT1
Feature Type ORF, Verified
Description ATP (CTP):tRNA-specific tRNA nucleotidyltransferase; different forms targeted to the nucleus, cytosol, and mitochondrion are generated via the use of multiple transcriptional and translational start sites (1 and see Summary Paragraph)
Name Description tRNA CCA-pyrophosphorylase 2
Chromosomal Location
ChrV:522669 to 521029 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Gene Ontology Annotations All CCA1 GO evidence and references
  View Computational GO annotations for CCA1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Mutant phenotypes All CCA1 Phenotype evidence and references
Classical genetics
conditional
reduction of function
Large-scale survey
conditional
null
reduction of function
Resources
interactions All CCA1 Interaction evidence and references
19 total interaction(s) for 17 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 3
  • Affinity Capture-Western: 1
  • Biochemical Activity: 1
  • Reconstituted Complex: 1
Genetic Interactions
  • Dosage Rescue: 1
  • Negative Genetic: 1
  • Positive Genetic: 8
  • Synthetic Growth Defect: 2
  • Synthetic Lethality: 1
Resources
Expression Summary
histogram
Resources
Protein Information All CCA1 Protein evidence and references
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrV:522669 to 521029 | 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..1641 522669..521029 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 SGDIDS000000970
SUMMARY PARAGRAPH for CCA1

CCA1 was first identified as a temperature sensitive mutant with elevated steady-state levels of some unstable mRNAs at the restrictive temperature (3). It encodes the ATP(CTP):tRNA nucleotidyl transferase, which adds 3'CCA termini to tRNAs (3). The stabilization of otherwise unstable transcripts in CCA1 mutants is probably due to a slowing of translational elongation that results from the presence of incompletely processed tRNAs (2). There are three in-frame ATGs at the start of the CCA1 gene, which result in the production of three isoforms, one located prodominantly in the mitochondria, the other two in both the nucleus and cytoplasm (1, 4, 5). For technical reasons, SGD sequence annotation currently includes only the longest form of CCA1. CCA1 has identifiable homologs in S. pombe, E. coli, and Arabidopsis (3).

Last updated: 1999-09-01

References cited on this page View Complete Literature Guide for CCA1
1) Chen JY, et al.  (1992) Cytoplasmic and mitochondrial tRNA nucleotidyltransferase activities are derived from the same gene in the yeast Saccharomyces cerevisiae. J Biol Chem 267(21):14879-83
2) Peltz SW, et al.  (1992) A mutation in the tRNA nucleotidyltransferase gene promotes stabilization of mRNAs in Saccharomyces cerevisiae. Mol Cell Biol 12(12):5778-84
3) Aebi M, et al.  (1990) Isolation of a temperature-sensitive mutant with an altered tRNA nucleotidyltransferase and cloning of the gene encoding tRNA nucleotidyltransferase in the yeast Saccharomyces cerevisiae. J Biol Chem 265(27):16216-20
4) Wolfe CL, et al.  (1994) Interplay of heterogeneous transcriptional start sites and translational selection of AUGs dictate the production of mitochondrial and cytosolic/nuclear tRNA nucleotidyltransferase from the same gene in yeast. J Biol Chem 269(18):13361-6
5) Wolfe CL, et al.  (1996) Mechanisms leading to and the consequences of altering the normal distribution of ATP(CTP):tRNA nucleotidyltransferase in yeast. J Biol Chem 271(9):4679-86