Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/82165
Title: Crystallization and X-ray diffraction analysis of the HMG domain of the chondrogenesis master regulator Sox9 in complex with a ChIP-Seq-identified DNA element
Authors: Vivekanandan, Saravanan
Moovarkumudalvan, Balasubramanian
Lescar, Julien
Kolatkar, Prasanna R.
Keywords: Sox9
Transcription factor
Issue Date: 2015
Source: Vivekanandan, S., Moovarkumudalvan, B., Lescar, J., & Kolatkar, P. R. (2015). Crystallization and X-ray diffraction analysis of the HMG domain of the chondrogenesis master regulator Sox9 in complex with a ChIP-Seq-identified DNA element. Acta Crystallographica Section F: Structural Biology Communications, 71(11), 1437-1441.
Series/Report no.: Acta Crystallographica Section F: Structural Biology Communications
Abstract: Sox9 is a fundamental sex-determining gene and the master regulator of chondrogenesis, and is involved in the development of various vital organs such as testes, kidney, heart and brain, and in skeletal development. Similar to other known Sox transcription factors, Sox9 recognizes and binds DNA with the consensus sequence C(T/A)TTG(T/A)(T/A) through the highly conserved HMG domain. Nonetheless, the molecular basis of the functional specificity of Sox9 in key developmental processes is still unclear. As an initial step towards a mechanistic understanding of Sox9 transcriptional regulation, the current work describes the details of the purification of the mouse Sox9 HMG domain (mSox9HMG), its crystallization in complex with a ChIP-Seq-identified FOXP2 promoter DNA element and the X-ray diffraction data analysis of this complex. The mSox9HMG-FOXP2 promoter DNA complex was crystallized by the hanging-drop vapour-diffusion method using 20% PEG 3350 in 200 mM sodium/potassium phosphate with 100 mM bis-tris propane at pH 8.5. The crystals diffracted to 2.7 Å resolution and the complex crystallized in the tetragonal space group P41212, with unit-cell parameters a = b = 99.49, c = 45.89 Å. Crystal-packing parameters revealed that asymmetric unit contained one mSox9HMG-FOXP2 promoter DNA complex with an estimated solvent content of 64%.
URI: https://hdl.handle.net/10356/82165
http://hdl.handle.net/10220/41126
ISSN: 2053-230X
DOI: 10.1107/S2053230X1501969X
Schools: School of Biological Sciences 
Rights: © 2015 International Union of Crystallography (IUCr). This paper was published in Acta Crystallographica Section F: Structural Biology Communications and is made available as an electronic reprint (preprint) with permission of International Union of Crystallography (IUCr). The published version is available at: [http://dx.doi.org/10.1107/S2053230X1501969X]. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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