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Molecular and Cellular Biology, January 1999, p. 835-845, Vol. 19, No. 1
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Two Xenopus Proteins That Bind the 3' End of Histone mRNA: Implications for Translational Control of Histone Synthesis during Oogenesis

Zeng-Feng Wang,1,2 Thomas C. Ingledue,1 Zbigniew Dominski,1,3 Ricardo Sanchez,1,3 and William F. Marzluff1,2,3,*

Program in Molecular Biology and Biotechnology,1 Department of Biology,2 and Department of Biochemistry and Biophysics,3 University of North Carolina, Chapel Hill, North Carolina 27599

Received 6 August 1998/Returned for modification 21 September 1998/Accepted 12 October 1998

Translationally inactive histone mRNA is stored in frog oocytes, and translation is activated at oocyte maturation. The replication-dependent histone mRNAs are not polyadenylated and end in a conserved stem-loop structure. There are two proteins (SLBPs) which bind the 3' end of histone mRNA in frog oocytes. SLBP1 participates in pre-mRNA processing in the nucleus. SLBP2 is oocyte specific, is present in the cytoplasm, and does not support pre-mRNA processing in vivo or in vitro. The stored histone mRNA is bound to SLBP2. As oocytes mature, SLBP2 is degraded and a larger fraction of the histone mRNA is bound to SLBP1. The mechanism of activation of translation of histone mRNAs may involve exchange of SLBPs associated with the 3' end of histone mRNA.

* Corresponding author. Mailing address: Program in Molecular Biology and Biotechnology, CB #7100, University of North Carolina, Chapel Hill, NC 27599. Phone: (919) 962-8920. Fax: (919) 966-6821. E-mail: marzluff{at}med.unc.edu.

Molecular and Cellular Biology, January 1999, p. 835-845, Vol. 19, No. 1
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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