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Nucleic Acids Research 2004 32(16):4833-4842; doi:10.1093/nar/gkh798
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Published online 9 September 2004

Nucleic Acids Research, Vol. 32 No. 16 © Oxford University Press 2004; all rights reserved

SLBP is associated with histone mRNA on polyribosomes as a component of the histone mRNP

Michael L. Whitfield1,2,4, Handan Kaygun2,3, Judith A. Erkmann1,2, W. H. Davin Townley-Tilson4, Zbigniew Dominski1,2 and William F. Marzluff1,2,3,*

1 Department of Biochemistry and Biophysics, 2 Program in Molecular Biology and Biotechnology, 3 Department of Biology, University of North Carolina, Chapel Hill, NC 27599, USA and 4 Department of Genetics, Dartmouth Medical School, Hanover, NH 03755, USA

* To whom correspondence should be addressed at Program in Molecular Biology and Biotechnology, University of North Carolina, Chapel Hill, NC 27599, USA. Tel: +1 919 962 8920; Fax: +1 919 966 6821; Email: marzluff{at}med.unc.edu

Received March 10, 2004; Revised May 10, 2004; Accepted August 10, 2004

The stem–loop binding protein (SLBP) binds the 3' end of histone mRNA and is present both in nucleus, and in the cytoplasm on the polyribosomes. SLBP participates in the processing of the histone pre-mRNA and in translation of the mature message. Histone mRNAs are rapidly degraded when cells are treated with inhibitors of DNA replication and are stabilized by inhibitors of translation, resulting in an increase in histone mRNA levels. Here, we show that SLBP is a component of the histone messenger ribonucleoprotein particle (mRNP). Histone mRNA from polyribosomes is immunoprecipitated with anti-SLBP. Most of the SLBP in cycloheximide-treated cells is present on polyribosomes as a result of continued synthesis and transport of the histone mRNP to the cytoplasm. When cells are treated with inhibitors of DNA replication, histone mRNAs are rapidly degraded but SLBP levels remain constant and SLBP is relocalized to the nucleus. SLBP remains active both in RNA binding and histone pre-mRNA processing when DNA replication is inhibited.


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