Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (268K) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (8)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Weisman-Shomer, P.
Right arrow Articles by Fry, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Weisman-Shomer, P.
Right arrow Articles by Fry, M.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2002, Vol. 30, No. 17 3672-3681
© 2002 Oxford University Press

Distinct domains in the CArG-box binding factor A destabilize tetraplex forms of the fragile X expanded sequence d(CGG)n

Pnina Weisman-Shomer, Esther Cohen and Michael Fry*

Unit of Biochemistry, Rappaport Faculty of Medicine, Technion—Israel Institute of Technology, PO Box 9649, Haifa 31096, Israel

*To whom correspondence should be addressed. Tel: +972 4 829 5328; Fax: +972 4 851 0735; Email: mickey{at}tx.technion.ac.il
The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors

Formation of hairpin or tetraplex structures of the FMR1 gene d(CGG)n sequence triggers its expansion, setting off fragile X syndrome. In searching for proteins that destabilize d(CGG)n secondary structures we purified from rat liver quadruplex telomeric DNA binding protein 42 (qTBP42) that disrupts G'2 bimolecular tetraplex d(CGG)n while paradoxically stabilizing the G'2 structure of the telomeric sequence d(TTAGGG)n. Based on peptide sequence homology of qTBP42 and mouse CArG-box binding factor A (CBF-A), we provide direct evidence that recombinant CBF-A protein is physically and immunochemically indistinguishable from qTBP42 and that it too destabilizes G'2 d(CGG)n while stabilizing G'2 d(TTAGGG)n. We inquired whether CBF-A employs the same or different domains to differentially interact with G'2 d(CGG)n and G'2 d(TTAGGG)n. Mutant CBF-A proteins that lack each or combinations of its five conserved motifs: RNP11, RNP12, RNP21, RNP22 and ATP/GTP-binding box were tested for their G'2 d(CGG)n destabilization and G'2 d(TTAGGG)n stabilization activities. We find that either RNP11 or the ATP/GTP motifs are necessary and sufficient for G'2 d(CGG)n destabilization whereas RNP21 suppresses destabilization by either one of these two motifs. Neither RNP11 nor the ATP/GTP motif are required for G'2 d(TTAGGG)n stabilization. Hence, CBF-A employs different domains to destabilize G'2 d(CGG)n or stabilize G'2 d(TTAGGG)n.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
Nucleic Acids ResHome page
A. Verma, V. K. Yadav, R. Basundra, A. Kumar, and S. Chowdhury
Evidence of genome-wide G4 DNA-mediated gene expression in human cancer cells
Nucleic Acids Res., July 13, 2009; (2009) gkn1076v2.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
N. Ofer, P. Weisman-Shomer, J. Shklover, and M. Fry
The quadruplex r(CGG)n destabilizing cationic porphyrin TMPyP4 cooperates with hnRNPs to increase the translation efficiency of fragile X premutation mRNA
Nucleic Acids Res., May 1, 2009; 37(8): 2712 - 2722.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
M. Paramasivam, A. Membrino, S. Cogoi, H. Fukuda, H. Nakagama, and L. E. Xodo
Protein hnRNP A1 and its derivative Up1 unfold quadruplex DNA in the human KRAS promoter: implications for transcription
Nucleic Acids Res., May 1, 2009; 37(9): 2841 - 2853.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
S. Khateb, P. Weisman-Shomer, I. Hershco-Shani, A. L. Ludwig, and M. Fry
The tetraplex (CGG)n destabilizing proteins hnRNP A2 and CBF-A enhance the in vivo translation of fragile X premutation mRNA
Nucleic Acids Res., September 27, 2007; 35(17): 5775 - 5788.
[Abstract] [Full Text] [PDF]


Home page
J BiochemHome page
H. Torigoe and A. Furukawa
Tetraplex Structure of Fission Yeast Telomeric DNA and Unfolding of the Tetraplex on the Interaction with Telomeric DNA Binding Protein Pot1
J. Biochem., January 1, 2007; 141(1): 57 - 68.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. Etzioni, A. Yafe, S. Khateb, P. Weisman-Shomer, E. Bengal, and M. Fry
Homodimeric MyoD Preferentially Binds Tetraplex Structures of Regulatory Sequences of Muscle-specific Genes
J. Biol. Chem., July 22, 2005; 280(29): 26805 - 26812.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
S. Khateb, P. Weisman-Shomer, I. Hershco, L. A. Loeb, and M. Fry
Destabilization of tetraplex structures of the fragile X repeat sequence (CGG)n is mediated by homolog-conserved domains in three members of the hnRNP family
Nucleic Acids Res., August 9, 2004; 32(14): 4145 - 4154.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
P. Weisman-Shomer, E. Cohen, I. Hershco, S. Khateb, O. Wolfovitz-Barchad, L. H. Hurley, and M. Fry
The cationic porphyrin TMPyP4 destabilizes the tetraplex form of the fragile X syndrome expanded sequence d(CGG)n
Nucleic Acids Res., July 15, 2003; 31(14): 3963 - 3970.
[Abstract] [Full Text] [PDF]



Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.