NGG1/YDR176W Summary Help

Standard Name NGG1
Systematic Name YDR176W
Alias ADA3 1 , SWI7 2
Feature Type ORF, Verified
Description Subunit of chromatin modifying histone acetyltransferase complexes; member of the ADA complex, the SAGA complex, and the SLIK complex; transcriptional regulator involved in glucose repression of Gal4p-regulated genes (3, 4, 5, 6 and see Summary Paragraph)
Chromosomal Location
ChrIV:814452 to 816560 | ORF Map | GBrowse
Gbrowse
Gene Ontology Annotations All NGG1 GO evidence and references
  View Computational GO annotations for NGG1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Targets 9 genes
Regulators 3 genes
Resources
Classical genetics
null
Large-scale survey
null
overexpression
Resources
288 total interaction(s) for 122 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 106
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 56
  • Biochemical Activity: 2
  • Co-fractionation: 4
  • Co-purification: 9
  • Reconstituted Complex: 8
  • Two-hybrid: 14

Genetic Interactions
  • Negative Genetic: 25
  • Phenotypic Enhancement: 1
  • Positive Genetic: 1
  • Synthetic Growth Defect: 48
  • Synthetic Lethality: 11
  • Synthetic Rescue: 2

Resources
Expression Summary
histogram
Resources
Length (a.a.) 702
Molecular Weight (Da) 79,281
Isoelectric Point (pI) 4.84
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrIV:814452 to 816560 | 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..2109 814452..816560 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 | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000002583
SUMMARY PARAGRAPH for NGG1

NGG1 (also called ADA3) encodes a component of three chromatin modifying histone acetyltransferase (HAT) complexes: SAGA, SLIK, and ADA (7, 8, 6; reviewed in 9). These complexes function in positive and negative transcriptional regulation of numerous RNA polymerase II-transcribed genes; in addition, SLIK plays a role in the retrograde response (6, 10; reviewed in 11). The three complexes each contain the histone acetyltransferase catalytic subunit Gcn5p, which interacts directly with Ada2p and preferentially modifies histones H3 and H2B (12; reviewed in 11). In vitro, Gcn5p acetylates N-terminal lysines on free histones, but acetylation of nucleosomal histone substrates also requires Ada2p and Ngg1p, which are found in a complex with Gcn5p (13). Ada2p has been shown to increase the HAT activity of Gcn5p, while Ngg1p plays a role in expanding the range of lysines that undergo acetylation (13).

Null mutations in NGG1 confer slow growth in minimal medium, no growth on any medium at 37 deg C, and resistance to the toxic effect of the chimeric transcriptional activator GAL4-VP16 (14). These null mutant phenotypes are complemented by the simultaneous expression of separate clones containing the NGG1 amino terminal half and carboxy terminal half, suggesting that Ngg1p has two domains and their covalent attachment is not required for function (7). The carboxy terminal domain interacts with Ada2p but not with Gcn5p in formation of the Ada2p-Ngg1p-Gcn5p complex (7). The amino terminal domain has been shown to interact with the transcriptional activation domains of Pdr1p and Prd3p (15), and is involved in transcriptional repression of the GAL genes by glucose (16).

Ngg1p is evolutionarily conserved among eukaryotes and orthologs have been described in several organisms, including Drosophila (17), Arabidopsis (18), and humans (19, 20). Human ADA3 interacts with p53 and is required for DNA damage-induced acetylation and consequent stabilization of p53 (21).

Last updated: 2010-03-26 Contact SGD

References cited on this page View Complete Literature Guide for NGG1
1) Berger SL, et al.  (1992) Genetic isolation of ADA2: a potential transcriptional adaptor required for function of certain acidic activation domains. Cell 70(2):251-65
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) Saleh A, et al.  (1997) Identification of native complexes containing the yeast coactivator/repressor proteins NGG1/ADA3 and ADA2. J Biol Chem 272(9):5571-8
4) Brandl CJ, et al.  (1993) Characterization of NGG1, a novel yeast gene required for glucose repression of GAL4p-regulated transcription. EMBO J 12(13):5255-65
5) Grant PA, et al.  (1998) A subset of TAF(II)s are integral components of the SAGA complex required for nucleosome acetylation and transcriptional stimulation. Cell 94(1):45-53
6) 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
7) Horiuchi J, et al.  (1995) ADA3, a putative transcriptional adaptor, consists of two separable domains and interacts with ADA2 and GCN5 in a trimeric complex. Mol Cell Biol 15(3):1203-9
8) Eberharter A, et al.  (1999) The ADA complex is a distinct histone acetyltransferase complex in Saccharomyces cerevisiae. Mol Cell Biol 19(10):6621-31
9) Sterner DE and Berger SL  (2000) Acetylation of histones and transcription-related factors. Microbiol Mol Biol Rev 64(2):435-59
10) 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
11) Daniel JA and Grant PA  (2007) Multi-tasking on chromatin with the SAGA coactivator complexes. Mutat Res 618(1-2):135-48
12) Marcus GA, et al.  (1994) Functional similarity and physical association between GCN5 and ADA2: putative transcriptional adaptors. EMBO J 13(20):4807-15
13) Balasubramanian R, et al.  (2002) Role of the Ada2 and Ada3 transcriptional coactivators in histone acetylation. J Biol Chem 277(10):7989-95
14) Pina B, et al.  (1993) ADA3: a gene, identified by resistance to GAL4-VP16, with properties similar to and different from those of ADA2. Mol Cell Biol 13(10):5981-9
15) Martens JA, et al.  (1996) Transcriptional activation by yeast PDR1p is inhibited by its association with NGG1p/ADA3p. J Biol Chem 271(27):15884-90
16) Brandl CJ, et al.  (1996) Structure/functional properties of the yeast dual regulator protein NGG1 that are required for glucose repression. J Biol Chem 271(16):9298-306
17) Kusch T, et al.  (2003) Two Drosophila Ada2 homologues function in different multiprotein complexes. Mol Cell Biol 23(9):3305-19
18) Stockinger EJ, et al.  (2001) Transcriptional adaptor and histone acetyltransferase proteins in Arabidopsis and their interactions with CBF1, a transcriptional activator involved in cold-regulated gene expression. Nucleic Acids Res 29(7):1524-33
19) Wang T, et al.  (2001) hADA3 is required for p53 activity. EMBO J 20(22):6404-13
20) Kumar A, et al.  (2002) Human papillomavirus oncoprotein E6 inactivates the transcriptional coactivator human ADA3. Mol Cell Biol 22(16):5801-12
21) Nag A, et al.  (2007) An essential role of human Ada3 in p53 acetylation. J Biol Chem 282(12):8812-20