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Nucleic Acids Research, 1992, Vol. 20, No. 5 1023-1030
© 1992

MOLECULAR BIOLOGY

Evolutionary conserved multiprotein complexes interact with the 3' untranslated region of histone transcripts

Richard Eckner* and Max L. Birnstiel

Research Institute of Molecular Pathology, Dr Bohr-Gasse 7 A-1030 Vienna, Austria

Received December 20, 1991. Revised February 10, 1992. Accepted February 10, 1992.

The replication dependent histone transcripts terminate with a highly conserved stem-loop structure. This feature distinguishes them from most other eukaryotlc mRNAs which end with a poly(A) tail. The 3' terminus of histone mRNA is a main determinant for rapid turnover of these transcripts. In this study, we report the Identification of two cytoplasmlc protein complexes that interact in a sequence specific fashion with 3' terminal sequences of a mouse histone H4 and a human histone H2A mRNA. The binding activities are conserved from frog to man. At least a fraction of one of the protein complexes appears to be specifically associated with polysomes. The evidence for an involvement of the observed protein complexes in turnover of histone transcripts is discussed.

*Present address: Dana Farber Cancer Institute, 44 Binney Street, Boston, MA 02115, USA


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