Structural analysis and dimerization profile of the SCAN domain of the pluripotency factor Zfp206
Huimei Hong, Felicia
Stanton, Lawrence W.
Kolatkar, Prasanna R.
KAUST DepartmentBioscience Core Lab
Online Publication Date2012-06-25
Print Publication Date2012-09
Permanent link to this recordhttp://hdl.handle.net/10754/334484
MetadataShow full item record
AbstractZfp206 (also named as Zscan10) belongs to the subfamily of C2H2 zinc finger transcription factors, which is characterized by the N-terminal SCAN domain. The SCAN domain mediates self-association and association between the members of SCAN family transcription factors, but the structural basis and selectivity determinants for complex formation is unknown. Zfp206 is important for maintaining the pluripotency of embryonic stem cells presumably by combinatorial assembly of itself or other SCAN family members on enhancer regions. To gain insights into the folding topology and selectivity determinants for SCAN dimerization, we solved the 1.85 crystal structure of the SCAN domain of Zfp206. In vitro binding studies using a panel of 20 SCAN proteins indicate that the SCAN domain Zfp206 can selectively associate with other members of SCAN family transcription factors. Deletion mutations showed that the N-terminal helix 1 is critical for heterodimerization. Double mutations and multiple mutations based on the Zfp206SCAN-Zfp110SCAN model suggested that domain swapped topology is a possible preference for Zfp206SCAN-Zfp110SCAN heterodimer. Together, we demonstrate that the Zfp206SCAN constitutes a protein module that enables C2H2 transcription factor dimerization in a highly selective manner using a domain-swapped interface architecture and identify novel partners for Zfp206 during embryonal development. 2012 The Author(s).
CitationLiang Y, Huimei Hong F, Ganesan P, Jiang S, Jauch R, et al. (2012) Structural analysis and dimerization profile of the SCAN domain of the pluripotency factor Zfp206. Nucleic Acids Research 40: 8721-8732. doi:10.1093/nar/gks611.
PublisherOxford University Press (OUP)
JournalNucleic Acids Research
PubMed Central IDPMC3458555
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Except where otherwise noted, this item's license is described as This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
- Crystal optimization and preliminary diffraction data analysis of the SCAN domain of Zfp206.
- Authors: Liang Y, Choo SH, Rossbach M, Baburajendran N, Palasingam P, Kolatkar PR
- Issue date: 2012 Apr 1
- Zfp206 is a transcription factor that controls pluripotency of embryonic stem cells.
- Authors: Wang ZX, Kueh JL, Teh CH, Rossbach M, Lim L, Li P, Wong KY, Lufkin T, Robson P, Stanton LW
- Issue date: 2007 Sep
- The structures of transcription factor CGL2947 from Corynebacterium glutamicum in two crystal forms: a novel homodimer assembling and the implication for effector-binding mode.
- Authors: Gao YG, Yao M, Itou H, Zhou Y, Tanaka I
- Issue date: 2007 Sep
- The dimerization domain of HNF-1alpha: structure and plasticity of an intertwined four-helix bundle with application to diabetes mellitus.
- Authors: Narayana N, Hua Q, Weiss MA
- Issue date: 2001 Jul 13
- Structure, function, and dynamics of the dimerization and DNA-binding domain of oncogenic transcription factor v-Myc.
- Authors: Fieber W, Schneider ML, Matt T, Kräutler B, Konrat R, Bister K
- Issue date: 2001 Apr 13
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