Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (378K) 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 (31)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Kolpashchikov, D. M.
Right arrow Articles by Lavrik, O. I.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kolpashchikov, D. M.
Right arrow Articles by Lavrik, O. I.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2001, Vol. 29, No. 2 373-379
© 2001 Oxford University Press

Polarity of human replication protein A binding to DNA

Dmitry M. Kolpashchikov1,2, Svetlana N. Khodyreva1, Denis Yu. Khlimankov1,2, Marc S. Wold3, Alain Favre2 and Olga I. Lavrik1,2,*

1Novosibirsk Institute of Bioorganic Chemistry, Siberian Division of Russian Academy of Sciences, Prospect Lavrentiev 8, 630090, Novosibirsk, Russia, 2Institut Jacques Monod CNRS, Universite Paris 6, Universite Paris 7, 75351 Paris Cedex 05, France and 3Department of Biochemistry, University of Iowa College of Medicine, 51 Newton Road, Iowa City, IA 52242-1109, USA

Replication protein A (RPA), the nuclear single-stranded DNA binding protein is involved in DNA replication, nucleotide excision repair (NER) and homologous recombination. It is a stable heterotrimer consisting of subunits with molecular masses of 70, 32 and 14 kDa (p70, p32 and p14, respectively). Gapped DNA structures are common intermediates during DNA replication and NER. To analyze the interaction of RPA and its subunits with gapped DNA we designed structures containing 9 and 30 nucleotide gaps with a photoreactive arylazido group at the 3'-end of the upstream oligonucleotide or at the 5'-end of the downstream oligonucleotide. UV crosslinking and subsequent analysis showed that the p70 subunit mainly interacts with the 5'-end of DNA irrespective of DNA structure, while the subunit orientation towards the 3'-end of DNA in the gap structures strongly depends on the gap size. The results are compared with the data obtained previously with the primer–template systems containing 5'- or 3'-protruding DNA strands. Our results suggest a model of polar RPA binding to the gapped DNA.

* To whom correspondence should be addressed at: Novosibirsk Institute of Bioorganic Chemistry, Siberian Division of Russian Academy of Sciences, Prospect Lavrentiev 8, 630090, Novosibirsk, Russia. Tel: +7 3832 344296; Fax: +7 3832 333677; Email: lavrik{at}niboch.nsc.ru


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
T. R. Salas, I. Petruseva, O. Lavrik, A. Bourdoncle, J.-L. Mergny, A. Favre, and C. Saintome
Human replication protein A unfolds telomeric G-quadruplexes
Nucleic Acids Res., October 18, 2006; 34(17): 4857 - 4865.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
E. Fanning, V. Klimovich, and A. R. Nager
A dynamic model for replication protein A (RPA) function in DNA processing pathways
Nucleic Acids Res., September 10, 2006; 34(15): 4126 - 4137.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. Weisshart, P. Pestryakov, R. W. P. Smith, H. Hartmann, E. Kremmer, O. Lavrik, and H.-P. Nasheuer
Coordinated Regulation of Replication Protein A Activities by Its Subunits p14 and p32
J. Biol. Chem., August 20, 2004; 279(34): 35368 - 35376.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
P. E. Pestryakov, D. Y. Khlimankov, E. Bochkareva, A. Bochkarev, and O. I. Lavrik
Human replication protein A (RPA) binds a primer-template junction in the absence of its major ssDNA-binding domains
Nucleic Acids Res., March 26, 2004; 32(6): 1894 - 1903.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. I. Arunkumar, M. E. Stauffer, E. Bochkareva, A. Bochkarev, and W. J. Chazin
Independent and Coordinated Functions of Replication Protein A Tandem High Affinity Single-stranded DNA Binding Domains
J. Biol. Chem., October 17, 2003; 278(42): 41077 - 41082.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
P. E. Pestryakov, K. Weisshart, B. Schlott, S. N. Khodyreva, E. Kremmer, F. Grosse, O. I. Lavrik, and H.-P. Nasheuer
Human Replication Protein A. THE C-TERMINAL RPA70 AND THE CENTRAL RPA32 DOMAINS ARE INVOLVED IN THE INTERACTIONS WITH THE 3'-END OF A PRIMER-TEMPLATE DNA
J. Biol. Chem., May 2, 2003; 278(19): 17515 - 17524.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
K. E. Sukhodolets, A. B. Hickman, S. K. Agarwal, M. V. Sukhodolets, V. H. Obungu, E. A. Novotny, J. S. Crabtree, S. C. Chandrasekharappa, F. S. Collins, A. M. Spiegel, et al.
The 32-Kilodalton Subunit of Replication Protein A Interacts with Menin, the Product of the MEN1 Tumor Suppressor Gene
Mol. Cell. Biol., January 15, 2003; 23(2): 493 - 509.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
G. Mass, T. Nethanel, O. I. Lavrik, M. S. Wold, and G. Kaufmann
Replication protein A modulates its interface with the primed DNA template during RNA-DNA primer elongation in replicating SV40 chromosomes
Nucleic Acids Res., September 15, 2001; 29(18): 3892 - 3899.
[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.