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Molecular and Cellular Biology, February 2007, p. 1531-1543, Vol. 27, No. 4
0270-7306/07/$08.00+0     doi:10.1128/MCB.00629-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Pur{alpha} and Purß Collaborate with Sp3 To Negatively Regulate ß-Myosin Heavy Chain Gene Expression during Skeletal Muscle Inactivity{triangledown}

Juan Ji,2 Gretchen L. Tsika,2 Hansjörg Rindt,2 Kathy L. Schreiber,1 John J. McCarthy,2 Robert J. Kelm Jr.,4 and Richard Tsika1,2,3*

Department of Biochemistry, School of Medicine,1 Department of Biomedical Sciences, School of Veterinary Medicine,2 Life Sciences Center, University of Missouri-Columbia, Columbia Missouri 65211,3 Department of Medicine, University of Vermont College of Medicine, Burlington, Vermont 054054

Received 11 April 2006/ Returned for modification 30 May 2006/ Accepted 23 November 2006

Adult skeletal muscle retains the capability of transcriptional reprogramming. This attribute is readily observable in the non-weight-bearing (NWB) soleus muscle, which undergoes a slow-to-fast fiber type transition concurrent with decreased ß-myosin heavy chain (ßMyHC) gene expression. Our previous work showed that Sp3 contributes to decreased ßMyHC gene expression under NWB conditions. In this study, we demonstrate that physical and functional interactions between Sp3, Pur{alpha}, and Purß proteins mediate repression of ßMyHC expression under NWB conditions. Binding of Pur{alpha} or Purß to the single-stranded ßMyHC distal negative regulatory element-sense strand (dßNRE-S) element is markedly increased under NWB conditions. Ectopic expression of Pur{alpha} and Purß decreased ßMyHC reporter gene expression, while mutation of the dßNRE-S element increased expression in C2C12 myotubes. The dßNRE-S element conferred Pur-dependent decreased expression on a minimal thymidine kinase promoter. Short interfering RNA sequences specific for Sp3 or for Pur{alpha} and Purß decreased endogenous Sp3 and Pur protein levels and increased ßMyHC reporter gene expression in C2C12 myotubes. Immunoprecipitation assays revealed an association between endogenous Pur{alpha}, Purß, and Sp3, while chromatin immunoprecipitation assays demonstrated Pur{alpha}, Purß, and Sp3 binding to the ßMyHC proximal promoter region harboring the dßNRE-S and C-rich elements in vivo. These data demonstrate that Pur proteins collaborate with Sp3 to regulate a transcriptional program that enables muscle cells to remodel their phenotype.

* Corresponding author. Mailing address: University of Missouri-Columbia, Biochemistry, 440D Life Sciences Center, 1201 Rollins Rd., Columbia, MO 65211. Phone: (573) 884-4547. Fax: (573) 884-3087. E-mail: tsikar{at}missouri.edu.

{triangledown} Published ahead of print on 4 December 2006.

Molecular and Cellular Biology, February 2007, p. 1531-1543, Vol. 27, No. 4
0270-7306/07/$08.00+0     doi:10.1128/MCB.00629-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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  • Yoshida, T. (2008). MCAT Elements and the TEF-1 Family of Transcription Factors in Muscle Development and Disease. Arterioscler. Thromb. Vasc. Bio. 28: 8-17 [Abstract] [Full Text]  
  • Knapp, A. M., Ramsey, J. E., Wang, S.-X., Strauch, A. R., Kelm, R. J. Jr. (2007). Structure-Function Analysis of Mouse Pur II: CONFORMATION ALTERING MUTATIONS DISRUPT SINGLE-STRANDED DNA AND PROTEIN INTERACTIONS CRUCIAL TO SMOOTH MUSCLE {alpha}-ACTIN GENE REPRESSION. J. Biol. Chem. 282: 35899-35909 [Abstract] [Full Text]  


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