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

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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-dependenthistone mRNAs are not polyadenylated and end in a conserved stem-loopstructure. There are two proteins (SLBPs) which bind the 3' endof histone mRNA in frog oocytes. SLBP1 participates in pre-mRNAprocessing in the nucleus. SLBP2 is oocyte specific, is presentin the cytoplasm, and does not support pre-mRNA processing invivo or in vitro. The stored histone mRNA is bound to SLBP2. Asoocytes mature, SLBP2 is degraded and a larger fraction of thehistone mRNA is bound to SLBP1. The mechanism of activation oftranslation of histone mRNAs may involve exchange of SLBPs associatedwith the 3' end of histonemRNA.

^* 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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