GTC
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE ADVANCED SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Genes to Cells (2007) 12, 171-182. doi:10.1111/j.1365-2443.2007.01042.x
© 2007 Blackwell Publishing or its licensors
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Similar articles in this journal
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Yamashita, K.
Right arrow Articles by Nishinakamura, R.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Yamashita, K.
Right arrow Articles by Nishinakamura, R.

Mouse homolog of SALL1, a causative gene for Townes–Brocks syndrome, binds to A/T-rich sequences in pericentric heterochromatin via its C-terminal zinc finger domains

Kazunari Yamashita1,2,a, Akira Sato3,4,a, Makoto Asashima4, Pi-Chao Wang2 and Ryuichi Nishinakamura1,3,*

1 Division of Integrative Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 860-0811, Japan
2 Division of Biological Functional Science, Graduate School of Life and Environmental Science, University of Tsukuba, Ibaraki 305-8572, Japan
3 Division of Stem Cell Regulation, The Institute of Medical Science, The University of Tokyo, Tokyo 108-8639, Japan
4 Department of Life Sciences, The University of Tokyo, Tokyo 153-8902, Japan

The Spalt (sal) gene family is conserved from Drosophila to humans. Mutations of human SALL1 cause Townes–Brocks syndrome, with features of ear, limb, anal, renal and heart anomalies. Sall1, a murine homolog of SALL1, is essential for kidney formation, and both Sall1 and SALL1 localize to heterochromatin in the nucleus. Here, we present a molecular mechanism for the heterochromatin localization of Sall1. Mutation analyses revealed that the 7th–10th C-terminal double zinc finger motifs were required for the localization. A recombinant protein of the most C-terminal double zinc finger (9th–10th) bound to specific A/T-rich sequences. Furthermore, Sall1 associated with A/T-rich sequences of the major satellite DNA in heterochromatin. Thus Sall1 may bind to A/T-rich sequences of the major satellite DNA via its C-terminal double zinc fingers, thereby mediating its localization to heterochromatin.

Communicated by: Tetsuya Taga

aThese two authors contributed equally to this work.

* Correspondence: E-mail: ryuichi{at}kaiju.medic.kumamoto-u.ac.jp




This article has been cited by other articles:


Home page
 DevelopmentHome page
Y. Kawakami, Y. Uchiyama, C. Rodriguez Esteban, T. Inenaga, N. Koyano-Nakagawa, H. Kawakami, M. Marti, M. Kmita, P. Monaghan-Nichols, R. Nishinakamura, et al.
Sall genes regulate region-specific morphogenesis in the mouse limb by modulating Hox activities
Development, February 15, 2009; 136(4): 585 - 594.
[Abstract] [Full Text] [PDF]

Home page
 Cereb CortexHome page
S. J. Harrison, R. Nishinakamura, and A. P. Monaghan
Sall1 Regulates Mitral Cell Development and Olfactory Nerve Extension in the Developing Olfactory Bulb
Cereb Cortex, July 1, 2008; 18(7): 1604 - 1617.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. M. Lauberth, A. C. Bilyeu, B. A. Firulli, K. L. Kroll, and M. Rauchman
A Phosphomimetic Mutation in the Sall1 Repression Motif Disrupts Recruitment of the Nucleosome Remodeling and Deacetylase Complex and Repression of Gbx2
J. Biol. Chem., November 30, 2007; 282(48): 34858 - 34868.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE ADVANCED SEARCH TABLE OF CONTENTS
Copyright © 2007 by Wiley-Blackwell Publishing.