Abstract
Dictyostelium discoideum Formin C (ForC) plays an important role in the fruiting body formation during the multicellular stages of the slime mold. Formins are multidomain proteins that are known to regulate the actin cytoskeleton. Here, we report the assignments of the 1H, 15N, and 13C nuclei of the N-terminal activation domain (residues 1–100) of ForC. Chemical shifts have been deposited at the BioMagResBank under the BMRB accession number 17,029. The N-terminal region of the 131 kDa ForC protein is supposed to form a GTPase-binding domain required for activation of the formin.
Similar content being viewed by others
References
Breuer S, Gerlach H, Kolaric B, Urbanke C, Opitz N, Geyer M (2006) Biochemical indication for myristoylation-dependent conformational changes in HIV-1 Nef. Biochemistry 45:2339–2349
Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6(3):277–293
Faix J, Grosse R (2006) Staying in shape with formins. Dev Cell 10(6):693–706
Grzesiek S, Anglister J, Bax A (1993) Correlation of backbone amide and aliphatic side-chain resonances in 13C/15N-enriched proteins by isotropic mixing of 13C magnetization. J Magn Reson B 101:114–119
Grzesiek S, Bax A, Hu JS, Kaufman J, Palmer I, Stahl SJ, Tjandra N, Wingfield PT (1997) Refined solution structure and backbone dynamics of HIV-1 Nef. Protein Sci 6(6):1248–1263
Higgs HN (2005) Formin proteins: a domain-based approach. Trends Biochem Sci 30(6):342–353
Johnson BR, Blevins RA (1994) NMRView: a computer program for the visualization and analysis of NMR data. J Biomol NMR 4:603–614
Kitayama C, Uyeda TQ (2003) ForC, a novel type of formin family protein lacking an FH1 domain, is involved in multicellular development in Dictyostelium discoideum. J Cell Sci 116(Pt 4):711–723
Schonichen A, Geyer M (2010) Fifteen formins for an actin filament: a molecular view on the regulation of human formins. Biochim Biophys Acta 1803(2):152–163
Schulte A, Stolp B, Schonichen A, Pylypenko O, Rak A, Fackler OT, Geyer M (2008) The human formin FHOD1 contains a bipartite structure of FH3 and GTPase-binding domains required for activation. Structure 16(9):1313–1323
Acknowledgments
We thank Diana Ludwig and Barbara Stopschinski for help in protein expression and purification. Prof. Dr. Stephan Grzesiek from the Biozentrum of the University of Basel in Switzerland, we thank for providing the NMR infrastructure as well as for general support to S.A.D. during her professional time in Basel. This work was supported by grants from the Deutsche Forschungsgemeinschaft to S.A.D. (DA 1195/3-1) and M.G. (GE 976/4-2).
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Dames, S.A., Schönichen, A. & Geyer, M. 1H, 15N, and 13C assignments of the N-terminal activation domain of Dictyostelium discoideum Formin C. Biomol NMR Assign 5, 47–49 (2011). https://doi.org/10.1007/s12104-010-9264-3
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s12104-010-9264-3