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Gene Review

ADA2  -  Ada2p

Saccharomyces cerevisiae S288c

Synonyms: D9461.33, Transcriptional adapter 2, YDR448W
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Disease relevance of ADA2

  • A selection for yeast mutants resistant to GAL4-VP16-induced toxicity previously identified two genes, ADA2 and ADA3, which may function as adaptors for some transcriptional activation domains and thereby facilitate activation [1].

High impact information on ADA2

  • Both the 0.8- and 1.8-MD Gcn5-containing complexes cofractionate with Ada2 and are lost in gcn5delta, ada2delta, or ada3delta yeast strains, illustrating that these HAT complexes are bona fide native Ada-transcriptional adaptor complexes [2].
  • This suggests that ADA2 and GCN5 are part of a heteromeric complex that mediates transcriptional activation [1].
  • Previously it was shown that yeast ADA2 protein is necessary for the full activity of some activation domains, such as VP16 and GCN4, in vivo and in vitro [3].
  • In addition, analysis of an ada2 rad6 deletion strain indicated that the SAGA acetyltransferase complex and Rad6 act in the same pathway to repress ARG1 in rich medium [4].
  • In the absence of Ada2p, the elution profile of Tra1p shifted to a distinct peak [5].

Biological context of ADA2


Associations of ADA2 with chemical compounds

  • Loss of either ADA2 or ADA3/NGG1 also affects a large number of genes and inhibits the rapid global increase in transcription that occurs in response to glucose [8].
  • The data presented here, together with our earlier data on the function of dAda2b, provide evidence that related Ada2 proteins of Drosophila, together with Gcn5 HAT, are involved in the acetylation of specific lysine residues in the N-terminal tails of nucleosomal H3 and H4 [10].

Physical interactions of ADA2


Enzymatic interactions of ADA2

  • The anti-silencing effect of Gcn5p is abolished by a mutation that eliminated its HAT activity or by deleting the ADA2 gene encoding a structural component of Gcn5p-containing HAT complexes [13].

Regulatory relationships of ADA2

  • A deletion of only the Ada2 SANT domain has exactly the same effect, strongly suggesting that Ada2 controls Gcn5 activity by virtue of its SANT domain [14].
  • This ability of ADA2 to activate transcription is mediated by ADA3, a gene with properties similar to ADA2 [3].

Other interactions of ADA2

  • Identification of native complexes containing the yeast coactivator/repressor proteins NGG1/ADA3 and ADA2 [15].
  • Deletion of GCN5 or ADA2 reduces repair at MET16 [16].
  • This suggests that a site required for ADA2p interaction lies between amino acids 308 and 373 and that ADA2p has a regulatory role in activation by GAL4p-NGG1p(1-373) [17].
  • Alterations in NOT2 contacts to ADA2, therefore, do not necessarily result in effects on the CCR4-NOT complex nor result in severe growth defects [12].
  • Although the activation domain of the yeast activator HAP4 is also highly negatively charged, its function is independent of at least one component of the adaptor complex, ADA2 [18].

Analytical, diagnostic and therapeutic context of ADA2


  1. Functional similarity and physical association between GCN5 and ADA2: putative transcriptional adaptors. Marcus, G.A., Silverman, N., Berger, S.L., Horiuchi, J., Guarente, L. EMBO J. (1994) [Pubmed]
  2. Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: characterization of an Ada complex and the SAGA (Spt/Ada) complex. Grant, P.A., Duggan, L., Côté, J., Roberts, S.M., Brownell, J.E., Candau, R., Ohba, R., Owen-Hughes, T., Allis, C.D., Winston, F., Berger, S.L., Workman, J.L. Genes Dev. (1997) [Pubmed]
  3. Yeast ADA2 protein binds to the VP16 protein activation domain and activates transcription. Silverman, N., Agapite, J., Guarente, L. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  4. The E2 ubiquitin conjugase Rad6 is required for the ArgR/Mcm1 repression of ARG1 transcription. Turner, S.D., Ricci, A.R., Petropoulos, H., Genereaux, J., Skerjanc, I.S., Brandl, C.J. Mol. Cell. Biol. (2002) [Pubmed]
  5. Tra1p is a component of the yeast Ada.Spt transcriptional regulatory complexes. Saleh, A., Schieltz, D., Ting, N., McMahon, S.B., Litchfield, D.W., Yates, J.R., Lees-Miller, S.P., Cole, M.D., Brandl, C.J. J. Biol. Chem. (1998) [Pubmed]
  6. Role for ADA/GCN5 products in antagonizing chromatin-mediated transcriptional repression. Pollard, K.J., Peterson, C.L. Mol. Cell. Biol. (1997) [Pubmed]
  7. ADR1 activation domains contact the histone acetyltransferase GCN5 and the core transcriptional factor TFIIB. Chiang, Y.C., Komarnitsky, P., Chase, D., Denis, C.L. J. Biol. Chem. (1996) [Pubmed]
  8. Regulation of gene expression by glucose in Saccharomyces cerevisiae: a role for ADA2 and ADA3/NGG1. Wu, M., Newcomb, L., Heideman, W. J. Bacteriol. (1999) [Pubmed]
  9. PfADA2, a Plasmodium falciparum homologue of the transcriptional coactivator ADA2 and its in vivo association with the histone acetyltransferase PfGCN5. Fan, Q., An, L., Cui, L. Gene (2004) [Pubmed]
  10. The Drosophila histone acetyltransferase gcn5 and transcriptional adaptor ada2a are involved in nucleosomal histone h4 acetylation. Ciurciu, A., Komonyi, O., Pankotai, T., Boros, I.M. Mol. Cell. Biol. (2006) [Pubmed]
  11. ADA3, a putative transcriptional adaptor, consists of two separable domains and interacts with ADA2 and GCN5 in a trimeric complex. Horiuchi, J., Silverman, N., Marcus, G.A., Guarente, L. Mol. Cell. Biol. (1995) [Pubmed]
  12. Characterization of mutations in NOT2 indicates that it plays an important role in maintaining the integrity of the CCR4-NOT complex. Russell, P., Benson, J.D., Denis, C.L. J. Mol. Biol. (2002) [Pubmed]
  13. A targeted histone acetyltransferase can create a sizable region of hyperacetylated chromatin and counteract the propagation of transcriptionally silent chromatin. Chiu, Y.H., Yu, Q., Sandmeier, J.J., Bi, X. Genetics (2003) [Pubmed]
  14. Multiple mechanistically distinct functions of SAGA at the PHO5 promoter. Barbaric, S., Reinke, H., Hörz, W. Mol. Cell. Biol. (2003) [Pubmed]
  15. Identification of native complexes containing the yeast coactivator/repressor proteins NGG1/ADA3 and ADA2. Saleh, A., Lang, V., Cook, R., Brandl, C.J. J. Biol. Chem. (1997) [Pubmed]
  16. Roles for Gcn5p and Ada2p in transcription and nucleotide excision repair at the Saccharomyces cerevisiae MET16 gene. Ferreiro, J.A., Powell, N.G., Karabetsou, N., Mellor, J., Waters, R. Nucleic Acids Res. (2006) [Pubmed]
  17. Structure/functional properties of the yeast dual regulator protein NGG1 that are required for glucose repression. Brandl, C.J., Martens, J.A., Margaliot, A., Stenning, D., Furlanetto, A.M., Saleh, A., Hamilton, K.S., Genereaux, J. J. Biol. Chem. (1996) [Pubmed]
  18. The acidic transcriptional activation domains of herpes virus VP16 and yeast HAP4 have different co-factor requirements. Wang, L., Turcotte, B., Guarente, L., Berger, S.L. Gene (1995) [Pubmed]
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