This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Beenders, B.
Right arrow Articles by Bellini, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Beenders, B.
Right arrow Articles by Bellini, M.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, April 2007, p. 2615-2624, Vol. 27, No. 7
0270-7306/07/$08.00+0     doi:10.1128/MCB.01968-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

The Tripartite Motif of Nuclear Factor 7 Is Required for Its Association with Transcriptional Units{triangledown}

Brent Beenders, Peter Lawrence Jones, and Michel Bellini*

Department of Cell and Developmental Biology, University of Illinois at Urbana—Champaign, Urbana, Illinois 61801

Received 19 October 2006/ Returned for modification 5 December 2006/ Accepted 16 January 2007

In amphibian oocytes, the maternal nuclear factor NF7 associates with the elongating pre-mRNAs present on the numerous lateral loops of the lampbrush chromosomes. Here, we have purified NF7 from an oocyte extract by using a combination of ion-exchange chromatography and gel filtration chromatography and demonstrated for the first time that nucleoplasmic NF7 exists primarily as free homotrimers. We confirmed the in vivo homotrimerization of NF7 by using a glutaraldehyde cross-linking assay, and we further showed that it only requires the coiled-coil domain of the NF7 tripartite motif/RBCC motif. Interestingly, we also obtained evidence that NF7 is recruited to the nucleus as a homotrimer, and expression of several mutated forms of NF7 in oocytes demonstrated that both the coiled coil and B box of NF7 are required for its chromosomal association. Together, these data strongly suggest that the interaction of NF7 with the active transcriptional units of RNA polymerase II is mediated by a trimeric B box. Finally, and in agreement with a role for NF7 in pre-mRNA maturation, we obtained evidence supporting the idea that NF7 associates with Cajal bodies.

* Corresponding author. Mailing address: Department of Cell and Developmental Biology, School of Molecular and Cellular Biology, 601 South Goodwin Avenue, Room B107 CLSL, Urbana, IL 61801. Phone: (217) 265-5297. Fax: (217) 244-6418. E-mail: bellini{at}life.uiuc.edu.

{triangledown} Published ahead of print on 29 January 2007.

Molecular and Cellular Biology, April 2007, p. 2615-2624, Vol. 27, No. 7
0270-7306/07/$08.00+0     doi:10.1128/MCB.01968-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Kim, M., Bellini, M., Ceman, S. (2009). Fragile X Mental Retardation Protein FMRP Binds mRNAs in the Nucleus. Mol. Cell. Biol. 29: 214-228 [Abstract] [Full Text]  
  • Li, X., Sodroski, J. (2008). The TRIM5{alpha} B-Box 2 Domain Promotes Cooperative Binding to the Retroviral Capsid by Mediating Higher-Order Self-Association. J. Virol. 82: 11495-11502 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»