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Gene Review

TCERG1  -  transcription elongation regulator 1

Homo sapiens

Synonyms: CA150, TAF2S, TATA box-binding protein-associated factor 2S, Transcription elongation regulator 1, Transcription factor CA150, ...
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Disease relevance of TCERG1

  • We further showed that CA150, a molecule that links transcription to splicing, interacts with the Tudor domain of the spinal muscular atrophy protein SMN in a CARM1-dependent fashion [1].

Psychiatry related information on TCERG1


High impact information on TCERG1

  • Human CA150, a transcriptional activator, binds to and is co-deposited with huntingtin during Huntington's disease [3].
  • The second WW domain of CA150 is a three-stranded beta-sheet that folds in vitro in microseconds and forms amyloid fibers under physiological conditions [3].
  • However, although CA150 is associated with the spliceosome, it appears to be dispensable for splicing in vitro [4].
  • Previous studies have demonstrated a role for SF1 in transcription repression, and we found that binding of the CA150 WW1 and WW2 domains to SF1 correlated exactly with the functional contribution of these domains for repression [5].
  • CA150 represses RNA polymerase II (RNAPII) transcription by inhibiting the elongation of transcripts [5].

Biological context of TCERG1


Associations of TCERG1 with chemical compounds

  • Our data suggest that abnormal expression of CA150, mediated by interaction with polyglutamine-expanded htt, may alter transcription and have a role in HD pathogenesis [8].

Physical interactions of TCERG1


Enzymatic interactions of TCERG1

  • In this model, CA150 binds to the phosphorylated CTD of elongating RNAPII and SF1 targets the nascent transcript [5].

Regulatory relationships of TCERG1

  • Together, our data indicate that mutant htt may induce CA150 dysfunction in striatal neurons and suggest that the restoration of nuclear protein cooperativity may be neuroprotective [6].

Other interactions of TCERG1

  • Specific alleles in GluR6 and CA150 locus were only observed in HD patients [9].
  • A protein that interacted directly with CA150 WW1 and WW2 was identified as the splicing-transcription factor SF1 [5].
  • The FF domain is a 60 amino acid residue phosphopeptide-binding module found in a variety of eukaryotic proteins including the transcription elongation factor CA150, the splicing factor Prp40 and p190RHOGAP [10].
  • Conspicuous accumulation of transcription elongation repressor hrp130/CA150 on the intron-rich Balbiani ring 3 gene [11].

Analytical, diagnostic and therapeutic context of TCERG1


  1. The Arginine Methyltransferase CARM1 Regulates the Coupling of Transcription and mRNA Processing. Cheng, D., C??t??, J., Shaaban, S., Bedford, M.T. Mol. Cell (2007) [Pubmed]
  2. Replication of twelve association studies for Huntington's disease residual age of onset in large Venezuelan kindreds. Andresen, J.M., Gay??n, J., Cherny, S.S., Brocklebank, D., Alkorta-Aranburu, G., Addis, E.A., Cardon, L.R., Housman, D.E., Wexler, N.S. J. Med. Genet. (2007) [Pubmed]
  3. General structural motifs of amyloid protofilaments. Ferguson, N., Becker, J., Tidow, H., Tremmel, S., Sharpe, T.D., Krause, G., Flinders, J., Petrovich, M., Berriman, J., Oschkinat, H., Fersht, A.R. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  4. The WW domain-containing proteins interact with the early spliceosome and participate in pre-mRNA splicing in vivo. Lin, K.T., Lu, R.M., Tarn, W.Y. Mol. Cell. Biol. (2004) [Pubmed]
  5. The transcription elongation factor CA150 interacts with RNA polymerase II and the pre-mRNA splicing factor SF1. Goldstrohm, A.C., Albrecht, T.R., Suñé, C., Bedford, M.T., Garcia-Blanco, M.A. Mol. Cell. Biol. (2001) [Pubmed]
  6. CA150 expression delays striatal cell death in overexpression and knock-in conditions for mutant huntingtin neurotoxicity. Arango, M., Holbert, S., Zala, D., Brouillet, E., Pearson, J., Régulier, E., Thakur, A.K., Aebischer, P., Wetzel, R., Déglon, N., Néri, C. J. Neurosci. (2006) [Pubmed]
  7. Identification of a co-repressor that inhibits the transcriptional and growth-arrest activities of CCAAT/enhancer-binding protein alpha. McFie, P.J., Wang, G.L., Timchenko, N.A., Wilson, H.L., Hu, X., Roesler, W.J. J. Biol. Chem. (2006) [Pubmed]
  8. The Gln-Ala repeat transcriptional activator CA150 interacts with huntingtin: neuropathologic and genetic evidence for a role in Huntington's disease pathogenesis. Holbert, S., Denghien, I., Kiechle, T., Rosenblatt, A., Wellington, C., Hayden, M.R., Margolis, R.L., Ross, C.A., Dausset, J., Ferrante, R.J., Néri, C. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  9. Modulation of age at onset in Huntington's disease and spinocerebellar ataxia type 2 patients originated from eastern India. Chattopadhyay, B., Ghosh, S., Gangopadhyay, P.K., Das, S.K., Roy, T., Sinha, K.K., Jha, D.K., Mukherjee, S.C., Chakraborty, A., Singhal, B.S., Bhattacharya, A.K., Bhattacharyya, N.P. Neurosci. Lett. (2003) [Pubmed]
  10. The structure of an FF domain from human HYPA/FBP11. Allen, M., Friedler, A., Schon, O., Bycroft, M. J. Mol. Biol. (2002) [Pubmed]
  11. Conspicuous accumulation of transcription elongation repressor hrp130/CA150 on the intron-rich Balbiani ring 3 gene. Sun, X., Zhao, J., Kylberg, K., Soop, T., Palka, K., Sonnhammer, E., Visa, N., Alzhanova-Ericsson, A.T., Daneholt, B. Chromosoma (2004) [Pubmed]
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