Skip Navigation


Nucleic Acids Research Advance Access originally published online on July 25, 2007
Nucleic Acids Research 2007 35(15):5073-5084; doi:10.1093/nar/gkm504
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (1812K) Freely available
Right arrow Screen PDF (664K) Freely available
Right arrow Supplementary Material
Right arrowOA All Versions of this Article:
35/15/5073    most recent
gkm504v1
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 (1)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Yamasaki, K.
Right arrow Articles by Harata, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yamasaki, K.
Right arrow Articles by Harata, K.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2007, Vol. 35, No. 15 5073-5084
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Structural Biology

Structural basis for recognition of the matrix attachment region of DNA by transcription factor SATB1

Kazuhiko Yamasaki1,*, Toshihiko Akiba2, Tomoko Yamasaki1 and Kazuaki Harata2

1Age Dimension Research Center and 2Biological Information Research Center, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Japan

*To whom correspondence should be addressed: Tel: +81 29 8619473; Fax: +81 29 8612706; Email: k-yamasaki{at}aist.go.jp

Received March 16, 2007. Revised June 11, 2007. Accepted June 11, 2007.

Special AT-rich sequence binding protein 1 (SATB1) regulates gene expression essential in immune T-cell maturation and switching of fetal globin species, by binding to matrix attachment regions (MARs) of DNA and inducing a local chromatin remodeling. Previously we have revealed a five-helix structure of the N-terminal CUT domain, which is essentially the folded region in the MAR-binding domain, of human SATB1 by NMR. Here we determined crystal structure of the complex of the CUT domain and a MAR DNA, in which the third helix of the CUT domain deeply enters the major groove of DNA in the B-form. Bases of 5'-CTAATA-3' sequence are contacted by this helix, through direct and water-mediated hydrogen bonds and apolar and van der Waals contacts. Mutations at conserved base-contacting residues, Gln402 and Gly403, reduced the DNA-binding activity, which confirmed the importance of the observed interactions involving these residues. A significant number of equivalent contacts are observed also for typically four-helix POU-specific domains of POU-homologous proteins, indicating that these domains share a common framework of the DNA-binding mode, recognizing partially similar DNA sequences.


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
P. K. Purbey, S. Singh, P. P. Kumar, S. Mehta, K. N. Ganesh, D. Mitra, and S. Galande
PDZ domain-mediated dimerization and homeodomain-directed specificity are required for high-affinity DNA binding by SATB1
Nucleic Acids Res., April 1, 2008; 36(7): 2107 - 2122.
[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.