open access

https://hdl.handle.net/2115/72478

Specific binding of heterogeneous ribonucleoprotein particle protein K to the human c-myc promoter, in vitro

英語

1993-08-25

American Society for Biochemistry and Molecular Biology

The Journal of biological chemistry

268(24)

18249-18258

A homopurine/homopyrimidine-like sequence is found 100-150 base pairs upstream of the human c-myc promoter P1. This element, termed the CT-element, has been shown to augment expression from P1, and it serves as a positive transcriptional element when coupled to a heterologous promoter in vivo and in vitro. Synthetic oligonucleotides comprising this element were used to form DNA-protein complexes in electrophoretic mobility shift assays. By using conventional and affinity methods, 61- and 34-kDa proteins were shown to be associated with these complexes. Amino acid sequence analysis and immunological methods have identified these proteins as heterogeneous ribonucleoprotein particle (hnRNP) proteins K and A1. Surprisingly, hnRNP protein K binds to the pyrimidine-rich strand of the CT-element in a sequence-specific manner as well as to the double-stranded molecule. Cotransfection of vectors encoding hnRNP protein K in the sense or anti-sense orientations with reporter plasmids driven by wild-type or mutant CT-elements demonstrates that hnRNP protein K augments gene expression in a cis-element-dependent manner. Taken together, these results suggest that hnRNP protein K may play a role in the transcriptional regulation of the human c-myc gene.

学術雑誌論文

Version of Record

This research was originally published in the Journal of Biological Chemistry. M Takimoto, T Tomonaga, M Matunis, M Avigan, H Krutzsch, G Dreyfuss and D Levens. Specific binding of heterogeneous ribonucleoprotein particle protein K to the human c-myc promoter, in vitro. J. Biol. Chem. 1993; 268:18249-18258. © the American Society for Biochemistry and Molecular Biology.

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