GCN5/YGR252W Summary Help

Standard Name GCN5 1
Systematic Name YGR252W
Alias ADA4 , SWI9 2 , AAS104 3
Feature Type ORF, Verified
Description Catalytic subunit of ADA and SAGA histone acetyltransferase complexes; modifies N-terminal lysines on histones H2B and H3; acetylates Rsc4p, a subunit of the RSC chromatin-remodeling complex, altering replication stress tolerance; relocalizes to the cytosol in response to hypoxia; mutant displays reduced transcription elongation in the G-less-based run-on (GLRO) assay; greater involvement in repression of RNAPII-dependent transcription than in activation (4, 5, 6, 7, 8, 9, 10 and see Summary Paragraph)
Name Description General Control Nonderepressible 11
Gene Product Alias KAT2 12
Chromosomal Location
ChrVII:996869 to 998188 | ORF Map | GBrowse
Gene Ontology Annotations All GCN5 GO evidence and references
  View Computational GO annotations for GCN5
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Targets 864 genes
Regulators 1 genes
Classical genetics
Large-scale survey
1006 total interaction(s) for 547 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 375
  • Affinity Capture-RNA: 2
  • Affinity Capture-Western: 70
  • Biochemical Activity: 34
  • Co-crystal Structure: 1
  • Co-localization: 5
  • Co-purification: 10
  • Protein-peptide: 1
  • Reconstituted Complex: 17
  • Two-hybrid: 5

Genetic Interactions
  • Dosage Growth Defect: 2
  • Dosage Lethality: 4
  • Dosage Rescue: 9
  • Negative Genetic: 178
  • Phenotypic Enhancement: 25
  • Phenotypic Suppression: 12
  • Positive Genetic: 37
  • Synthetic Growth Defect: 106
  • Synthetic Lethality: 79
  • Synthetic Rescue: 34

Expression Summary
Length (a.a.) 439
Molecular Weight (Da) 51,069
Isoelectric Point (pI) 6.63
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrVII:996869 to 998188 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1320 996869..998188 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 SGDIDS000003484

GCN5 encodes a histone acetyltransferase (HAT) that functions as a coactivator in transcriptional regulation (13 and reviewed in 14). Gcn5p has been shown to target N-terminal lysine residues K11/K16 and K9/K14/K18/K23/K27 in histones H2B and H3 respectively; alone it only acts on free histones, however, in association with HAT complexes Gcn5p acetylates nucleosomal histones (15, 16, 17, 18). Gcn5p is the catalytic subunit of three chromatin modifying complexes: ADA, SAGA, and SLIK/SALSA, which are involved in the retrograde response as well as both positive and negative transcriptional regulation of numerous genes (17, 19, 20, 21, 22 and reviewed in 14 and 23).

Functional domains of Gcn5p include a C-terminal bromodomain, which is required for SAGA-mediated nucleosomal acetylation, the HAT domain, and an Ada2p interaction domain (19, 24, 25). Ada2p is a transcriptional coactivator, also found in ADA, SAGA, and SLIK/SALSA, whose presence enhances Gcn5p HAT activity (24, 26). Gcn5p-containing HAT complexes are recruited to specific promoters by the transcriptional activator Gcn4p (27, 28). Although it does not affect the enzyme's in vitro activity, post-translational modification of Gcn5p by sumoylation has also been suggested to contribute to the regulation of transcription (29).

Although histone H4 is not a direct target of Gcn5p in vivo, GCN5 deletion results in decreased acetylation of H4 sites (30). gcn5 mutations also cause disruption of chromatin structure, transcriptional defects at promoter regions, and meiotic arrest in diploid cells (31, 32, 33). Homologs of Gcn5p have been identified in Toxoplasma gondii, S. pombe, Tetrahymena, Arabidopsis, Drosophila, mouse, and human. Mammals have two Gcn5p homologs, the closely related proteins GCN5L2 (OMIM) and p300/CREB-binding protein-associated factor (PCAF; OMIM) (reviewed in 4).

Last updated: 2006-04-25 Contact SGD

References cited on this page View Complete Literature Guide for GCN5
1) Georgakopoulos T and Thireos G  (1992) Two distinct yeast transcriptional activators require the function of the GCN5 protein to promote normal levels of transcription. EMBO J 11(11):4145-52
2) Breeden L and Nasmyth K  (1987) Cell cycle control of the yeast HO gene: cis- and trans-acting regulators. Cell 48(3):389-97
3) Thireos G, et al.  (1984) 5' untranslated sequences are required for the translational control of a yeast regulatory gene. Proc Natl Acad Sci U S A 81(16):5096-100
4) Sterner DE and Berger SL  (2000) Acetylation of histones and transcription-related factors. Microbiol Mol Biol Rev 64(2):435-59
5) Langer MR, et al.  (2001) Mutational analysis of conserved residues in the GCN5 family of histone acetyltransferases. J Biol Chem 276(33):31321-31
6) VanDemark AP, et al.  (2007) Autoregulation of the rsc4 tandem bromodomain by gcn5 acetylation. Mol Cell 27(5):817-28
7) Charles GM, et al.  (2011) Site-specific acetylation mark on an essential chromatin-remodeling complex promotes resistance to replication stress. Proc Natl Acad Sci U S A 108(26):10620-5
8) Tous C, et al.  (2011) A novel assay identifies transcript elongation roles for the Nup84 complex and RNA processing factors. EMBO J 30(10):1953-64
9) Ghosh Dastidar R, et al.  (2012) The nuclear localization of SWI/SNF proteins is subjected to oxygen regulation. Cell Biosci 2(1):30
10) Lanza AM, et al.  (2012) Linking yeast Gcn5p catalytic function and gene regulation using a quantitative, graded dominant mutant approach. PLoS One 7(4):e36193
11) Lucchini G, et al.  (1984) Positive regulatory interactions of the HIS4 gene of Saccharomyces cerevisiae. Mol Cell Biol 4(7):1326-33
12) Allis CD, et al.  (2007) New nomenclature for chromatin-modifying enzymes. Cell 131(4):633-6
13) Brownell JE, et al.  (1996) Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation. Cell 84(6):843-51
14) Lee TI and Young RA  (2000) Transcription of eukaryotic protein-coding genes. Annu Rev Genet 34:77-137
15) Suka N, et al.  (2001) Highly specific antibodies determine histone acetylation site usage in yeast heterochromatin and euchromatin. Mol Cell 8(2):473-9
16) Zhang W, et al.  (1998) Essential and redundant functions of histone acetylation revealed by mutation of target lysines and loss of the Gcn5p acetyltransferase. EMBO J 17(11):3155-67
17) Grant PA, et al.  (1997) Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: characterization of an Ada complex and the SAGA (Spt/Ada) complex. Genes Dev 11(13):1640-50
18) Ruiz-Garcia AB, et al.  (1997) Gcn5p is involved in the acetylation of histone H3 in nucleosomes. FEBS Lett 403(2):186-90
19) Sterner DE, et al.  (1999) Functional organization of the yeast SAGA complex: distinct components involved in structural integrity, nucleosome acetylation, and TATA-binding protein interaction. Mol Cell Biol 19(1):86-98
20) Pray-Grant MG, et al.  (2002) The novel SLIK histone acetyltransferase complex functions in the yeast retrograde response pathway. Mol Cell Biol 22(24):8774-86
21) Sterner DE, et al.  (2002) SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates with activated transcription. Proc Natl Acad Sci U S A 99(18):11622-7
22) Lee TI, et al.  (2000) Redundant roles for the TFIID and SAGA complexes in global transcription. Nature 405(6787):701-4
23) Jacobson SJ, et al.  (2004) Functional analyses of chromatin modifications in yeast. Methods Enzymol 377:3-55
24) Candau R, et al.  (1997) Histone acetyltransferase activity and interaction with ADA2 are critical for GCN5 function in vivo. EMBO J 16(3):555-65
25) Sterner DE, et al.  (2002) The SANT domain of Ada2 is required for normal acetylation of histones by the yeast SAGA complex. J Biol Chem 277(10):8178-86
26) Syntichaki P and Thireos G  (1998) The Gcn5.Ada complex potentiates the histone acetyltransferase activity of Gcn5. J Biol Chem 273(38):24414-9
27) Kuo MH, et al.  (2000) Gcn4 activator targets Gcn5 histone acetyltransferase to specific promoters independently of transcription. Mol Cell 6(6):1309-20
28) Qiu H, et al.  (2005) Interdependent recruitment of SAGA and Srb mediator by transcriptional activator Gcn4p. Mol Cell Biol 25(9):3461-74
29) Sterner DE, et al.  (2006) Sumoylation of the yeast Gcn5 protein. Biochemistry 45(3):1035-42
30) Grant PA, et al.  (1999) Expanded lysine acetylation specificity of Gcn5 in native complexes. J Biol Chem 274(9):5895-900
31) Gregory PD, et al.  (1998) Absence of Gcn5 HAT activity defines a novel state in the opening of chromatin at the PHO5 promoter in yeast. Mol Cell 1(4):495-505
32) Perez-Martin J and Johnson AD  (1998) Mutations in chromatin components suppress a defect of Gcn5 protein in Saccharomyces cerevisiae. Mol Cell Biol 18(2):1049-54
33) Burgess SM, et al.  (1999) GCN5-dependent histone H3 acetylation and RPD3-dependent histone H4 deacetylation have distinct, opposing effects on IME2 transcription, during meiosis and during vegetative growth, in budding yeast. Proc Natl Acad Sci U S A 96(12):6835-40