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Molecular and Cellular Biology, June 2000, p. 4188-4198, Vol. 20, No. 12
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Stem-Loop Binding Protein, the Protein That Binds the 3' End of Histone mRNA, Is Cell Cycle Regulated by Both Translational and Posttranslational Mechanisms

Michael L. Whitfield,1 Lian-Xing Zheng,1 Amy Baldwin,2 Tomohiko Ohta,3,dagger Myra M. Hurt,2 and William F. Marzluff1,3,4,*

Department of Biochemistry and Biophysics,1 Program in Molecular Biology and Biotechnology,4 and Lineberger Comprehensive Cancer Center,3 University of North Carolina, Chapel Hill, North Carolina, and Department of Biological Sciences, Florida State University, Tallahassee, Florida2

Received 8 March 2000/Accepted 23 March 2000

The expression of the replication-dependent histone mRNAs is tightly regulated during the cell cycle. As cells progress from G1 to S phase, histone mRNA levels increase 35-fold, and they decrease again during G2 phase. Replication-dependent histone mRNAs are the only metazoan mRNAs that lack polyadenylated tails, ending instead in a conserved stem-loop. Much of the cell cycle regulation is posttranscriptional and is mediated by the 3' stem-loop. A 31-kDa stem-loop binding protein (SLBP) binds the 3' end of histone mRNA. The SLBP is necessary for pre-mRNA processing and accompanies the histone mRNA to the cytoplasm, where it is a component of the histone messenger RNP. We used synchronous CHO cells selected by mitotic shakeoff and HeLa cells synchronized at the G1/S or the M/G1 boundary to study the regulation of SLBP during the cell cycle. In each system the amount of SLBP is regulated during the cell cycle, increasing 10- to 20-fold in the late G1 and then decreasing in the S/G2 border. SLBP mRNA levels are constant during the cell cycle. SLBP is regulated at the level of translation as cells progress from G1 to S phase, and the protein is rapidly degraded as they progress into G2. Regulation of SLBP may account for the posttranscriptional component of the cell cycle regulation 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.

dagger On leave from Department of Surgery, St. Marianna University School of Medicine, Kawasaki 216, Japan.


Molecular and Cellular Biology, June 2000, p. 4188-4198, Vol. 20, No. 12
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.



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