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Molecular and Cellular Biology, September 2006, p. 6702-6712, Vol. 26, No. 17
0270-7306/06/$08.00+0     doi:10.1128/MCB.00391-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

ZFP100, a Component of the Active U7 snRNP Limiting for Histone Pre-mRNA Processing, Is Required for Entry into S Phase

Eric J. Wagner and William F. Marzluff*

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

Received 6 March 2006/ Returned for modification 3 April 2006/ Accepted 29 June 2006

Metazoan replication-dependent histone mRNAs are the only eukaryotic mRNAs that are not polyadenylated. The cleavage of histone pre-mRNA to form the unique 3' end requires the U7 snRNP and the stem-loop binding protein (SLBP) that binds the 3' end of histone mRNA. U7 snRNP contains three novel proteins, Lsm10 and Lsm11, which are part of the core U7 Sm complex, and ZFP100, a Zn finger protein that helps stabilize binding of the U7 snRNP to the histone pre-mRNA by interacting with the SLBP/pre-mRNA complex. Using a reporter gene that encodes a green fluorescent protein mRNA ending in a histone 3' end and mimics histone gene expression, we demonstrate that ZFP100 is the limiting factor for histone pre-mRNA processing in vivo. The overexpression of Lsm10 and Lsm11 increases the cellular levels of U7 snRNP but has no effect on histone pre-mRNA processing, while increasing the amount of ZFP100 increases histone pre-mRNA processing but has no effect on U7 snRNP levels. We also show that knocking down the known components of U7 snRNP by RNA interference results in a reduction in cell growth and an unsuspected cell cycle arrest in early G1, suggesting that active U7 snRNP is necessary to allow progression through G1 phase to S phase.

* 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) 962-1274. E-mail: marzluff{at}med.unc.edu.

Molecular and Cellular Biology, September 2006, p. 6702-6712, Vol. 26, No. 17
0270-7306/06/$08.00+0     doi:10.1128/MCB.00391-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Sullivan, K. D., Mullen, T. E., Marzluff, W. F., Wagner, E. J. (2009). Knockdown of SLBP results in nuclear retention of histone mRNA. RNA 15: 459-472 [Abstract] [Full Text]  
  • Cakmakci, N. G., Lerner, R. S., Wagner, E. J., Zheng, L., Marzluff, W. F. (2008). SLIP1, a Factor Required for Activation of Histone mRNA Translation by the Stem-Loop Binding Protein. Mol. Cell. Biol. 28: 1182-1194 [Abstract] [Full Text]  
  • Mullen, T. E., Marzluff, W. F. (2008). Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'. Genes Dev. 22: 50-65 [Abstract] [Full Text]  


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