Abstract

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. NANOG, Sox2 and Oct4 are transcription factors with key functions in mammalian stem cell biology. They are central of pluripotency in ES cells. Loss of NANOG induces differentiation towards an endoderm-like lineage in embryonic stem (ES) cells, whereas forced expression retains the ES phenotype in the absence of the otherwise essential growth factors. NANOG binds to promoter elements of hundreds of target genes and regulates their expression. The mechanism of this transcriptional regulation is not yet known. Currently, one X-ray crystal structure of the homeodomain of murine Nanog is available in the PDB;however, numerous studies have shown that the pathways maintaining pluripotency are different between human and mouse ES cells. We plan to determine the structure and DNA binding studies of NANOG, Sox2 and Oct4 by NMR.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR002301-26
Application #
8361239
Study Section
Special Emphasis Panel (ZRG1-BCMB-H (40))
Project Start
2011-03-01
Project End
2012-02-29
Budget Start
2011-03-01
Budget End
2012-02-29
Support Year
26
Fiscal Year
2011
Total Cost
$8,041
Indirect Cost

  Institution

Name
University of Wisconsin Madison
Department
Biochemistry
Type
Schools of Earth Sciences/Natur
DUNS #
161202122
City
Madison
State
WI
Country
United States
Zip Code
53715

  Publications

Travers, Timothy; López, Cesar A; Van, Que N et al. (2018) Molecular recognition of RAS/RAF complex at the membrane: Role of RAF cysteine-rich domain. Sci Rep 8:8461
Thomas, Nathan E; Wu, Chao; Morrison, Emma A et al. (2018) The C terminus of the bacterial multidrug transporter EmrE couples drug binding to proton release. J Biol Chem 293:19137-19147
Assadi-Porter, Fariba M; Radek, James; Rao, Hongyu et al. (2018) Multimodal Ligand Binding Studies of Human and Mouse G-Coupled Taste Receptors to Correlate Their Species-Specific Sweetness Tasting Properties. Molecules 23:
Wijayatunga, Nadeeja N; Sams, Valerie G; Dawson, John A et al. (2018) Roux-en-Y gastric bypass surgery alters serum metabolites and fatty acids in patients with morbid obesity. Diabetes Metab Res Rev 34:e3045
Assadi-Porter, Fariba M; Reiland, Hannah; Sabatini, Martina et al. (2018) Metabolic Reprogramming by 3-Iodothyronamine (T1AM): A New Perspective to Reverse Obesity through Co-Regulation of Sirtuin 4 and 6 Expression. Int J Mol Sci 19:
Dominguez, Eddie; Zarnowski, Robert; Sanchez, Hiram et al. (2018) Conservation and Divergence in the Candida Species Biofilm Matrix Mannan-Glucan Complex Structure, Function, and Genetic Control. MBio 9:
Franco, Aldo; Dovell, Sanaz; Möller, Carolina et al. (2018) Structural plasticity of mini-M conotoxins - expression of all mini-M subtypes by Conus regius. FEBS J 285:887-902
Wales, Jessica A; Chen, Cheng-Yu; Breci, Linda et al. (2018) Discovery of stimulator binding to a conserved pocket in the heme domain of soluble guanylyl cyclase. J Biol Chem 293:1850-1864
Selen Alpergin, Ebru S; Bolandnazar, Zeinab; Sabatini, Martina et al. (2017) Metabolic profiling reveals reprogramming of lipid metabolic pathways in treatment of polycystic ovary syndrome with 3-iodothyronamine. Physiol Rep 5:
Mong, Surin K; Cochran, Frank V; Yu, Hongtao et al. (2017) Heterochiral Knottin Protein: Folding and Solution Structure. Biochemistry 56:5720-5725

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