Skip Navigation

This Article
Right arrow Print PDF (5637K)
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 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 (14)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Barrijal, S.
Right arrow Articles by Rommelaere, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Barrijal, S.
Right arrow Articles by Rommelaere, J.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1992, Vol. 20, No. 19 5053-5060
© 1992

GENOME STRUCTURE AND MAPPING

Nucleolin forms a specific complex with a fragment of the viral (minus) strand of minute virus of mice DNA

Saïd Barrijal1, Manoussos Manoussos2, Zhennan Gu1, Bernard L. Avalosse1, Pascale Belenguer3, Francois Amalric3 and Jean Rommelaere1,2,*

1Laboratory of Biophysics and Radiobiology, Department of Molecular Biology, Université Libre de Bruxelles B-1640 Rhode St Genèse, Belgium 2Molecular Oncology Unit CNRS URA 1160, Institut Pasteur de Lille, F-59019 Lille Cédex, France 3Laboratory of Biochemistry and Cellular Genetics CNRS CNRS, 31062 Toulouse Cédex, France

* To whom correspondence should be addressed

Received July 13, 1992. Revised August 10, 1992. Accepted August 10, 1992.

Nucleolin, a major nucleolar protein, forms a specific complex with the genome (a single-stranded DNA molecule of minus polarity) of parvovlrus MVMp in vitro. By means of South-western blotting experiments, we mapped the binding site to a 222-nucleotide motif within the non-structural transcription unit, referred to as NUBE (nucleolln-blnding element). The specificity of the interaction was confirmed by competitive gel retardation assays. DNasel and nuclease S1 probing showed that NUBE folds into a secondary structure, in agreement with a computer-assisted conformational prediction. The whole NUBE may be necessary for the interaction with nucleolin, as suggested by the failure of NUBE subfragments to bind the protein and by the nuclease footprinting experiments. The present work extends the previously reported ability of nucleolin to form a specific complex with ribosomal RNA, to a defined DNA substrate. Considering the tropism of MVMp DNA replication for host cell nucleoll, these data raise the possibility that nucleolin may contribute to the regulation of the parvoviral life-cycle.


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
 J. Virol.Home page
S. R. Opie, K. H. Warrington Jr., M. Agbandje-McKenna, S. Zolotukhin, and N. Muzyczka
Identification of Amino Acid Residues in the Capsid Proteins of Adeno-Associated Virus Type 2 That Contribute to Heparan Sulfate Proteoglycan Binding
J. Virol., June 15, 2003; 77(12): 6995 - 7006.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
C. Cziepluch, S. Lampel, A. Grewenig, C. Grund, P. Lichter, and J. Rommelaere
H-1 Parvovirus-Associated Replication Bodies: a Distinct Virus-Induced Nuclear Structure
J. Virol., May 15, 2000; 74(10): 4807 - 4815.
[Abstract] [Full Text]

Home page
 FASEB J.Home page
M. Srivastava and H. B. Pollard
Molecular dissection of nucleolin's role in growth and cell proliferation: new insights
FASEB J, November 1, 1999; 13(14): 1911 - 1922.
[Abstract] [Full Text]

Home page
 J. Cell Sci.Home page
H Ginisty, H Sicard, B Roger, and P Bouvet
Structure and functions of nucleolin
J. Cell Sci., January 3, 1999; 112(6): 761 - 772.
[Abstract] [PDF]

Home page
 J. Biol. Chem.Home page
S. H. E. Zaidi and J. S. Malter
Nucleolin and Heterogeneous Nuclear Ribonucleoprotein C Proteins Specifically Interact with the 3`-Untranslated Region of Amyloid Protein Precursor mRNA
J. Biol. Chem., July 21, 1995; 270(29): 17292 - 17298.
[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.