Skip Navigation

This Article
Right arrow Print PDF (7803K)
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 (31)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Mazin, A.
Right arrow Articles by Devoret, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mazin, A.
Right arrow Articles by Devoret, R.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1994, Vol. 22, No. 20 4335-4341
© 1994

MOLECULAR BIOLOGY

Kin17, a mouse nuclear zinc finger protein that binds preferentially to curved DNA

Alexander Mazin$, Tatiana Timchenko1, Josiane Ménissier-de Murcia1,ø, Valérie Schreiber1,ø, Jaime F. Angulo2,§, Murcia Gilbert de1,ø and Raymond Devoret*

G.E. Mutagenése et Cancérogenese, Institut Curie, Bâtiment 110, Centre Universitaire, F-91405 Orsay 1UPR 9003, Cancérogenèse et Mutagenèse Moléculaire et Structurale, Institut de Biologie Moléculaire et Cellulaire CNRS, 15 rue Descartes, F-67084 Strasbourg 2G.E.Mutagenèse et Cancerogénèse Laboratoire d'Enzymologie CNRS, F-91198 Gif sur Yvette, France

*To whom correspondence should be addressed

Received April 5, 1994. Revised August 24, 1994. Accepted August 24, 1994.

Kin17 is a 45 kDa protein encoded by the KIN17 gene located on mouse chromosome 2, band A. The kin17 amino acid sequence predicts two domains, which were shown to be functional: (i) a bipartite nuclear localization signal (NLS) that can drive the protein to the cell nucleus, (ii) a bona fide zinc finger of the C2H2 type. The zinc finger is involved in kin17 binding to double-stranded DNA since a mutant deleted of the zinc finger, kin17{delta}1, showed reduced binding. Singlestranded DNA was bound poorly by kin17. Interestingly, we found that kin17 protein showed preferential binding to curved DNA from either pBR322 or synthetic oligonucleotides. Binding of kin17 to a non-curved DNA segment increased after we had inserted into it a short curved synthetic oligonucleotide. Kin17{delta}2, a mutant deleted of 110 amino acids at the C-terminal end, still exhibited preferential binding to curved DNA and so did kin17{delta}1, suggesting that a domain recognizing curved DNA is located in the protein core.

$Section of Microbiology, Hutchison Hall, University of California at Davis, DAVIS, CA 95616-8665, USA,

§Laboratoire de Cytométrie Départ. Pathol. & Toxicol. Experimentales, D.S.V., C. E. A., BP 6, F-92265 Fontenay Aux Roses and

øUPR 9003, Cancérogenese et Mutagenése Moléculaire et Structurale, Pôle API ESBS/CNRS, Boulevard Sébastien Brandt, F-67400 Illkirch, France


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
 Protein Sci.Home page
L. Carlier, J. Couprie, A. le Maire, L. Guilhaudis, I. Milazzo-Segalas, M. Courcon, M. Moutiez, M. Gondry, D. Davoust, B. Gilquin, et al.
Solution structure of the region 51 160 of human KIN17 reveals an atypical winged helix domain
Protein Sci., December 1, 2007; 16(12): 2750 - 2755.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
L. Miccoli, I. Frouin, O. Novac, D. Di Paola, F. Harper, M. Zannis-Hadjopoulos, G. Maga, D. S. F. Biard, and J. F. Angulo
The Human Stress-Activated Protein kin17 Belongs to the Multiprotein DNA Replication Complex and Associates In Vivo with Mammalian Replication Origins
Mol. Cell. Biol., May 1, 2005; 25(9): 3814 - 3830.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
G. Pinon-Lataillade, C. Masson, J. Bernardino-Sgherri, V. Henriot, P. Mauffrey, Y. Frobert, S. Araneda, and J. F. Angulo
KIN17 encodes an RNA-binding protein and is expressed during mouse spermatogenesis
J. Cell Sci., July 15, 2004; 117(16): 3691 - 3702.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
L. Miccoli, D. S. F. Biard, I. Frouin, F. Harper, G. Maga, and J. F. Angulo
Selective interactions of human kin17 and RPA proteins with chromatin and the nuclear matrix in a DNA damage- and cell cycle-regulated manner
Nucleic Acids Res., July 15, 2003; 31(14): 4162 - 4175.
[Abstract] [Full Text] [PDF]

Home page
 Mol Cancer ResHome page
D. S.F. Biard, L. Miccoli, E. Despras, F. Harper, E. Pichard, C. Creminon, and J. F. Angulo
Participation of kin17 Protein in Replication Factories and in Other DNA Transactions Mediated by High Molecular Weight Nuclear Complexes
Mol. Cancer Res., May 1, 2003; 1(7): 519 - 531.
[Abstract] [Full Text] [PDF]

Home page
 Cancer Res.Home page
L. Miccoli, D. S. F. Biard, C. Creminon, and J. F. Angulo
Human Kin17 Protein Directly Interacts with the Simian Virus 40 Large T Antigen and Inhibits DNA Replication
Cancer Res., October 1, 2002; 62(19): 5425 - 5435.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. S. F. Biard, L. Miccoli, E. Despras, Y. Frobert, C. Creminon, and J. F. Angulo
Ionizing Radiation Triggers Chromatin-bound kin17 Complex Formation in Human Cells
J. Biol. Chem., May 17, 2002; 277(21): 19156 - 19165.
[Abstract] [Full Text] [PDF]

Home page
 CarcinogenesisHome page
P. Kannouche, P. Mauffrey, G. Pinon-Lataillade, M. G. Mattei, A. Sarasin, L. Daya-Grosjean, and J. F. Angulo
Molecular cloning and characterization of the human KIN17 cDNA encoding a component of the UVC response that is conserved among metazoans
Carcinogenesis, September 1, 2000; 21(9): 1701 - 1710.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
P Kannouche and J. Angulo
Overexpression of kin17 protein disrupts nuclear morphology and inhibits the growth of mammalian cells
J. Cell Sci., January 10, 1999; 112(19): 3215 - 3224.
[Abstract] [PDF]

Home page
 Mol. Cell. Biol.Home page
M. Masson, C. Niedergang, V. Schreiber, S. Muller, J. Menissier-de Murcia, and G. de Murcia
XRCC1 Is Specifically Associated with Poly(ADP-Ribose) Polymerase and Negatively Regulates Its Activity following DNA Damage
Mol. Cell. Biol., June 1, 1998; 18(6): 3563 - 3571.
[Abstract] [Full Text]


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.