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Title: Deciphering the Sox-Oct partner code by quantitative cooperativity measurements
Authors: Prabhakar, Shyam
Jauch, Ralf
Ng, Calista K. L.
Li, Noel X.
Chee, Sheena.
Kolatkar, Prasanna R.
Keywords: DRNTU::Science::Biological sciences
Issue Date: 2012
Source: Ng, C. K. L., Li, N. X., Chee, S., Prabhakar, S., Kolatkar, P. R., & Jauch, R. (2012). Deciphering the Sox-Oct partner code by quantitative cooperativity measurements. Nucleic acids research, 40(11), 4933-4941.
Series/Report no.: Nucleic acids research
Abstract: Several Sox-Oct transcription factor (TF) combinations have been shown to cooperate on diverse enhancers to determine cell fates. Here, we developed a method to quantify biochemically the Sox-Oct cooperation and assessed the pairing of the high-mobility group (HMG) domains of 11 Sox TFs with Oct4 on a series of composite DNA elements. This way, we clustered Sox proteins according to their dimerization preferences illustrating that Sox HMG domains evolved different propensities to cooperate with Oct4. Sox2, Sox14, Sox21 and Sox15 strongly cooperate on the canonical element but compete with Oct4 on a recently discovered compressed element. Sry also cooperates on the canonical element but binds additively to the compressed element. In contrast, Sox17 and Sox4 cooperate more strongly on the compressed than on the canonical element. Sox5 and Sox18 show some cooperation on both elements, whereas Sox8 and Sox9 compete on both elements. Testing rationally mutated Sox proteins combined with structural modeling highlights critical amino acids for differential Sox-Oct4 partnerships and demonstrates that the cooperativity correlates with the efficiency in producing induced pluripotent stem cells. Our results suggest selective Sox-Oct partnerships in genome regulation and provide a toolset to study protein cooperation on DNA.
DOI: 10.1093/nar/gks153
Rights: © 2012 The Authors. This paper was published in Nucleic Acids Research and is made available as an electronic reprint (preprint) with permission of the authors. The paper can be found at the following official DOI: []. 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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