Skip Navigation

This Article
Right arrow Print PDF (3226K)
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 Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Muraiso, T.
Right arrow Articles by Kominami, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Muraiso, T.
Right arrow Articles by Kominami, R.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1992, Vol. 20, No. 24 6631-6635
© 1992

MOLECULAR BIOLOGY

A single-stranded DNA binding protein from mouse tumor cells specifically recognizes the C-rich strand of the (AGG:CCT)n repeats that can alter DNA conformation

Tomoe Muraiso, Shigetoshi Nomoto, Hajime Yamazaki, Yukio Mishima and Ryo Kominami*

First Department of Biochemistry, Niigata University School of Medicine Asahimachi-dori 1-757, Niigata 951, Japan

*To whom correspondence should be addressed

Received August 28, 1992. Revised November 16, 1992. Accepted November 16, 1992.

A protein that binds to a synthetic oligonucleotide of (CCT)12 has been purified from Ehrlich ascltes tumor cells by a (CCT)12 affinity chromatography. The protein (p70) has an apparent molecular mass of 70 kDa, as assayed by Southwestern analysis. A competition experiment revealed that p70 binds to (CCT)12 (CCCT)8 and (CCTCCCT)6 but not to (CTT)12 (CT)16 and (CCTGCCT)6 suggesting that p70 has a sequence-specificity. The complementary (AGG)12 and the double stranded DNA did not show the binding. It is also confirmed by S1 nuclease analysis that the (AGG:CCT)12 duplex takes a single-stranded conformation in the absence of the protein. This raises a possibility that the duplex forms two single-stranded loops in chromosomes, the C-rich strand being bound to p70. Structural analysis of the resulting (AGG)12 strand by non-denaturing polyacrylamide gel electrophoresis demonstrated the presence of slower and faster migrated conformers in a neutral pH buffer containing 50 mM NaCl at 5°C. The ratio was dependent on the DNA concentration. Both conformers disappeared in the absence of NaCl. This suggests that (AGG)12 can form intra- and inter-molecular complexes by non-Watson-Crick, guanine:guanine base-pairing. The possible biological function of the (AGG:CCT)n duplex and the p70 is discussed.


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. Biol. Chem.Home page
Y. Mishima, H. Kaizu, and R. Kominami
Pairing of DNA Fragments Containing (GGA:TCC)n Repeats and Promotion by High Mobility Group Protein 1 and Histone H1
J. Biol. Chem., October 17, 1997; 272(42): 26578 - 26584.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. L. Nelson, N. A. Becker, G. S. Pahwa, M. A. Hollingsworth, and L. J. Maher III
Potential for H-DNA in the Human MUC1 Mucin Gene Promoter
J. Biol. Chem., July 26, 1996; 271(30): 18061 - 18067.
[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.