CTA1/YDR256C Summary Help

Standard Name CTA1 1
Systematic Name YDR256C
Feature Type ORF, Verified
Description Catalase A; breaks down hydrogen peroxide in the peroxisomal matrix formed by acyl-CoA oxidase (Pox1p) during fatty acid beta-oxidation (2 and see Summary Paragraph)
Name Description CaTalase A 1
Chromosomal Location
ChrIV:969680 to 968133 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gene Ontology Annotations All CTA1 GO evidence and references
  View Computational GO annotations for CTA1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 3 genes
Classical genetics
Large-scale survey
40 total interaction(s) for 37 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 1
  • Affinity Capture-RNA: 2
  • Affinity Capture-Western: 1
  • Biochemical Activity: 1
  • Protein-peptide: 1
  • Reconstituted Complex: 6
  • Two-hybrid: 7

Genetic Interactions
  • Dosage Rescue: 2
  • Negative Genetic: 12
  • Phenotypic Enhancement: 1
  • Positive Genetic: 2
  • Synthetic Lethality: 4

Expression Summary
Length (a.a.) 515
Molecular Weight (Da) 58,555
Isoelectric Point (pI) 7.46
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrIV:969680 to 968133 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1548 969680..968133 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 SGDIDS000002664

CTA1 encodes catalase A, which is involved in hydrogen peroxide detoxification in the peroxisomal and mitochondrial matrices (1, 3). In peroxisomes, the primary source of hydrogen peroxide is that produced during fatty acid beta-oxidation (1, 4, and reviewed in 2). In mitochondria, hydrogen peroxide is produced by the superoxide dismutases Sod1p and Sod2p in defending against reactive oxygen species (5). Catalases break down hydrogen peroxide into dioxygen (02) and water molecules (reviewed in 6). Cta1p activity is important during oxidative stress response and in protecting proteins against oxidative inactivation (7, 8). Cta1p activity is also increased during caloric restriction and during oxidative stress caused by the processes of aging, acid stress adaptation, and thermotolerance (9, 10, 11).

Catalase A is a homotetramer with one heme group and one NADP(H) cofactor binding site per subunit (4). Transcription of CTA1 is regulated in response to oleic acid, glucose, heme, and oxygen, (12, 13, 14). This transcriptional response is mediated by the transcriptional activators Adr1p, Oaf1p, Rtg1p, and Rtg2p via binding to overlapping ORE and UAS1 elements in the CTA1 promoter (15, 16 and references therein).

The S. cerevisiae genome encodes a second catalase, cytoplasmic catalase T (encoded by CTT1), and although these two enzymes are functionally similar, Cta1p is more similar in sequence to the peroxiosomal catalases from the cow Bos taurus and the pathogenic yeast Candida tropicalis than it is to Ctt1p (17).

Last updated: 2008-07-02 Contact SGD

References cited on this page View Complete Literature Guide for CTA1
1) Cohen G, et al.  (1985) Isolation of the catalase A gene of Saccharomyces cerevisiae by complementation of the cta1 mutation. Mol Gen Genet 200(1):74-9
2) Hiltunen JK, et al.  (2003) The biochemistry of peroxisomal beta-oxidation in the yeast Saccharomyces cerevisiae. FEMS Microbiol Rev 27(1):35-64
3) Petrova VY, et al.  (2004) Dual targeting of yeast catalase A to peroxisomes and mitochondria. Biochem J 380(Pt 2):393-400
4) Mate MJ, et al.  (1999) Structure of catalase-A from Saccharomyces cerevisiae. J Mol Biol 286(1):135-49
5) Sturtz LA, et al.  (2001) A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage. J Biol Chem 276(41):38084-9
6) Jamieson DJ  (1998) Oxidative stress responses of the yeast Saccharomyces cerevisiae. Yeast 14(16):1511-27
7) Kurita O  (2003) Overexpression of peroxisomal malate dehydrogenase MDH3 gene enhances cell death on H2O2 stress in the ald5 mutant of Saccharomyces cerevisiae. Curr Microbiol 47(3):192-7
8) Lushchak VI and Gospodaryov DV  (2005) Catalases protect cellular proteins from oxidative modification in Saccharomyces cerevisiae. Cell Biol Int 29(3):187-92
9) Agarwal S, et al.  (2005) Caloric restriction augments ROS defense in S. cerevisiae, by a Sir2p independent mechanism. Free Radic Res 39(1):55-62
10) Giannattasio S, et al.  (2005) Acid stress adaptation protects Saccharomyces cerevisiae from acetic acid-induced programmed cell death. Gene 354():93-8
11) Davidson JF, et al.  (1996) Oxidative stress is involved in heat-induced cell death in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 93(10):5116-21
12) Skoneczny M and Rytka J  (2000) Oxygen and haem regulate the synthesis of peroxisomal proteins: catalase A, acyl-CoA oxidase and Pex1p in the yeast Saccharomyces cerevisiae; the regulation of these proteins by oxygen is not mediated by haem. Biochem J 350 Pt 1():313-9
13) Rytka J, et al.  (1978) Haemoprotein formation in yeast. III. The role of carbon catabolite repression in the regulation of catalase A and T formation. Mol Gen Genet 160(1):51-7
14) Hortner H, et al.  (1982) Regulation of synthesis of catalases and iso-1-cytochrome c in Saccharomyces cerevisiae by glucose, oxygen and heme. Eur J Biochem 128(1):179-84
15) Chelstowska A and Butow RA  (1995) RTG genes in yeast that function in communication between mitochondria and the nucleus are also required for expression of genes encoding peroxisomal proteins. J Biol Chem 270(30):18141-6
16) Gurvitz A, et al.  (2001) Saccharomyces cerevisiae Adr1p governs fatty acid beta-oxidation and peroxisome proliferation by regulating POX1 and PEX11. J Biol Chem 276(34):31825-30
17) Cohen G, et al.  (1988) Sequence of the Saccharomyces cerevisiae CTA1 gene and amino acid sequence of catalase A derived from it. Eur J Biochem 176(1):159-63