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Nucleic Acids Research, 1988, Vol. 16, No. 6 2473-2487
© 1988

Articles

Characterization by human antibodies of two HeLa cell proteins which are related to Xenopus laevis transcription factor TFIIIA

Sylvie Lagaye*, Jean-Philippe Barque, Marc le Maire1, Herman Denis1 and Christian-Jacques Larsen

U-301 INSERM, Centre Hayem, Hôpital Saint-Louis 1 avenue Claude Vellefaux, 75475 Paris Cedex 10, France 1Centre de Génétique Moléculaire, Centre National de la Recherche Scientifique F-91 190 Gif-sur-Yvette, France

*To whom reprint request should be sent

Received December 29, 1987. Revised February 17, 1988. Accepted February 17, 1988.

The sera of two patients with autoimmune disorders recognize in HeLa cell extracts two proteins with apparent molecular masses of 37,000 (p37) daltons and 32,000 daltons (p32). These proteins are non covalently associated with 5S RNA and sediment as 7–10 S particles in sucrose density gradients. Both proteins are antigenetically related to TFIIIA, a previously described protein of Xenopus laevis which is known as a 5S RNA transcription factor and occurs in oocytes as a noncovalent complex with 5S RNA. Like TFIIIA, HeLa cell proteins p37 binds in vitro to 5S RNA and to cloned 5S RNA genes. These results suggest that protein p37 fulfils in HeLa cells a function similar to that of TFIIIA in amphibian oocytes, ie control of 5S RNA transcription.


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