This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Gomez-Cuadrado, A.
Right arrow Articles by Ruiz-Carrillo, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gomez-Cuadrado, A.
Right arrow Articles by Ruiz-Carrillo, A.

 Previous Article  |  Next Article 

Mol. Cell. Biol., Dec 1995, 6670-6685, Vol 15, No. 12
Copyright © 1995, American Society for Microbiology

Initiation binding repressor, a factor that binds to the transcription initiation site of the histone h5 gene, is a glycosylated member of a family of cell growth regulators [corrected] [published erratum appears in Mol Cell Biol 1996 Feb;16(2):735]

A Gomez-Cuadrado, M Martin, M Noel and A Ruiz-Carrillo
Cancer Research Center, Medical School of Laval University, L'Hotel- Dieu de Quebec, Canada.

Initiation binding repressor [corrected] (IBR) is a chicken erythrocyte factor (apparent molecular mass, 70 to 73 kDa) that binds to the sequences spanning the transcription initiation site of the histone h5 gene, repressing its transcription. A variety of other cells, including transformed erythroid precursors, do not have IBR but a factor referred to as IBF (68 to 70 kDa) that recognizes the same IBR sites. We have cloned the IBR cDNA and studied the relationship of IBR and IBF. IBR is a 503-amino-acid-long acidic protein which is 99.0% identical to the recently reported human NRF-1/alpha-Pal factor and highly related to the invertebrate transcription factors P3A2 and erected wing gene product (EWG). We present evidence that IBR and IBF are most likely identical proteins, differing in their degree of glycosylation. We have analyzed several molecular aspects of IBR/F and shown that the factor associates as stable homodimers and that the dimer is the relevant DNA- binding species. The evolutionarily conserved N-terminal half of IBR/F harbors the DNA-binding/dimerization domain (outer limits, 127 to 283), one or several casein kinase II sites (37 to 67), and a bipartite nuclear localization signal (89 to 106) which appears to be necessary for nuclear targeting. Binding site selection revealed that the alternating RCGCRYGCGY consensus constitutes high-affinity IBR/F binding sites and that the direct-repeat palindrome TGCGCATGCGCA is the optimal site. A survey of genes potentially regulated by this family of factors primarily revealed genes involved in growth-related metabolism.


This article has been cited by other articles:

  • Hossain, M. B., Ji, P., Anish, R., Jacobson, R. H., Takada, S. (2009). Poly(ADP-ribose) Polymerase 1 Interacts with Nuclear Respiratory Factor 1 (NRF-1) and Plays a Role in NRF-1 Transcriptional Regulation. J. Biol. Chem. 284: 8621-8632 [Abstract] [Full Text]  
  • Scarpulla, R. C. (2008). Transcriptional Paradigms in Mammalian Mitochondrial Biogenesis and Function. Physiol. Rev. 88: 611-638 [Abstract] [Full Text]  
  • Tokusumi, Y., Zhou, S., Takada, S. (2004). Nuclear Respiratory Factor 1 Plays an Essential Role in Transcriptional Initiation from the Hepatitis B Virus X Gene Promoter. J. Virol. 78: 10856-10864 [Abstract] [Full Text]  
  • Chang, W.-T., Huang, A-M. (2004). {alpha}-Pal/NRF-1 Regulates the Promoter of the Human Integrin-associated Protein/CD47 Gene. J. Biol. Chem. 279: 14542-14550 [Abstract] [Full Text]  
  • Solecki, D., Bernhardt, G., Lipp, M., Wimmer, E. (2000). Identification of a Nuclear Respiratory Factor-1 Binding Site within the Core Promoter of the human polio virus receptor/CD155 Gene. J. Biol. Chem. 275: 12453-12462 [Abstract] [Full Text]  
  • Amsterdam, A., Burgess, S., Golling, G., Chen, W., Sun, Z., Townsend, K., Farrington, S., Haldi, M., Hopkins, N. (1999). A large-scale insertional mutagenesis screen in zebrafish. Genes Dev. 13: 2713-2724 [Abstract] [Full Text]  
  • Bogarad, L. D., Arnone, M. I., Chang, C., Davidson, E. H. (1998). Interference with gene regulation in living sea urchin embryos: Transcription factor Knock Out (TKO), a genetically controlled vector for blockade of specific transcription factors. Proc. Natl. Acad. Sci. USA 95: 14827-14832 [Abstract] [Full Text]  
  • Becker, T., Burgess, S., Amsterdam, A., Allende, M., Hopkins, N (1998). not really finished is crucial for development of the zebrafish outer retina and encodes a transcription factor highly homologous to human Nuclear Respiratory Factor-1 and avian Initiation Binding Repressor. Development 125: 4369-4378 [Abstract]  
  • Weber, J. R. M., Skene, J. H. P. (1997). Identification of a Novel Repressive Element That Contributes to Neuron-Specific Gene Expression. J. Neurosci. 17: 7583-7593 [Abstract] [Full Text]  
  • Gugneja, S., Scarpulla, R. C. (1997). Serine Phosphorylation within a Concise Amino-terminal Domain in Nuclear Respiratory Factor 1 Enhances DNA Binding. J. Biol. Chem. 272: 18732-18739 [Abstract] [Full Text]  
  • Amsterdam, A., Yoon, C., Allende, M., Becker, T., Kawakami, K., Burgess, S., Gaiano, N., Hopkins, N. (1997). Retrovirus-mediated Insertional Mutagenesis in Zebrafish and Identification of a Molecular Marker for Embryonic Germ Cells. Cold Spring Harb Symp Quant Biol 62: 437-450 [Abstract]  
  • Chang, Q., Su, K., Baker, J. R., Yang, X., Paterson, A. J., Kudlow, J. E. (2000). Phosphorylation of Human Glutamine:Fructose-6-phosphate Amidotransferase by cAMP-dependent Protein Kinase at Serine 205 Blocks the Enzyme Activity. J. Biol. Chem. 275: 21981-21987 [Abstract] [Full Text]  
  • Fazio, I. K., Bolger, T. A., Gill, G. (2001). Conserved Regions of the Drosophila Erect Wing Protein Contribute Both Positively and Negatively to Transcriptional Activity. J. Biol. Chem. 276: 18710-18716 [Abstract] [Full Text]