The sequence-specific nuclear matrix binding factor F6 is a chicken GATA-like protein

@article{Vassetzky1993TheSN,
  title={The sequence-specific nuclear matrix binding factor F6 is a chicken GATA-like protein},
  author={Yegor S Vassetzky and Cl{\'a}udia Vit{\'o}ria de Moura Gallo and A. N. Bogdanova and Sergey V Razin and Klaus Scherrer},
  journal={Molecular and General Genetics MGG},
  year={1993},
  volume={238},
  pages={309-314}
}
The sequence-specific DNA-binding protein factor F6, which binds upstream of the cluster of the chicken α-globin genes, has previously been found to interact with a DNA fragment containing a replication origin and a nuclear matrix binding site. This protein has been partially characterized. Based on its molecular weight and binding affinity, F6 belongs to a family of GATA proteins, the chicken equivalent of transcription factor NFE-1. An oligonucleotide including the binding site for F6… CONTINUE READING

From This Paper

Figures, tables, and topics from this paper.
5 Citations
38 References
Similar Papers

References

Publications referenced by this paper.
Showing 1-10 of 38 references

Excision close to matrix attachment regions of the whole domain of the chicken alpha globin genes by nuclease SI and characterization of the framing structures

  • F Recillas Targa, SV Razin, CV De Moura Gallo, K Scherrer
  • Proc Natl Acad Sci USA,
  • 1993

Marcaud L (1993a) Silencer and enhancer elements placed at the 3'-side of the chicken and duck alpha globin gene

  • F Recillas Targa, CV De Moura Galla, M Huesca, K Scherrer
  • domains. Gene,
  • 1993

Laemmli UK (1992) In vivo topoisomerase II cleavage of the Drosophila histone and satellite II repeats DNA sequence and structural characteristics

  • E Kis
  • EMBO J
  • 1992

The presence of sequence - specific protein binding sites correlate with replication activity and matrix binding in a 1 . 7 Kb - long DNA fragment of the chicken alpha - globin gene domain

  • CV DeMouraGallo, YS Vassetzky, M Huesca, K Scherrer
  • Biochem Biophys Res Com
  • 1992

Similar Papers

Loading similar papers…