Nucleic Acids Research, 1994, Vol. 22, No. 22 4660-4666
© 1994
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Changes in the stem-loop at the 3' terminus of histone mRNA affects its nucleocytoplasmic transport and cytoplasmic regulation
1Program in Molecular Biolgoy and Biotechnology, University of North CArolina Chapel Hill, NC 27599, USA 2Department of Biochemistry and Biophysics, University of North CArolina Chapel Hill, NC 27599, USA 3Curriculum in Genetics and Molecular Biology, University of North CArolina Chapel Hill, NC 27599, USA 4Department of Biology, University of North CArolina Chapel Hill, NC 27599, USA
*To whom correspondence should be addressed at: Program in Molecular Biology. CBS7100. University of North Carolina. Chapel Hill. NC 27599. USA
Received July 19, 1994. Revised September 24, 1994. Accepted September 24, 1994.
The stem-loop structure at the 3' end of replicationdependent histone mRNA is required for efficient premRNA processing, localization of histone mRNA to the polyribosomes, and regulation of histone mRNA degradation. A protein, the stem-loop binding protein (SLBP), binds the 3' end of histone mRNA and is thought to mediate some or all of these processes. A mutant histone mRNA with two nucleotide changes in the loop was constructed and found to be transported inefficiently to the cytoplasm. The mutant histone mRNA, unlike the wild-type histone mRNA, was not rapidly degraded when DNA synthesis is inhibited, and was not stabilized upon inhibition of protein synthesis. The stem-loop binding protein (SLBP) has between a 20–50 fold greater affinity for the wild type histone stem-loop structure than for the mutant stem-loop structure, suggesting that the alteration in the efficiency of transport and the normal degradation pathway in histone mRNA may be due to the reduced affinity of the mutant stem-loop for the SLBP.
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