@article{33147f4c57d64721b69713ddd8405b46,
title = "She2p is a novel RNA binding protein with a basic helical hairpin motif",
abstract = "Selective transport of mRNAs in ribonucleoprotein particles (mRNP) ensures asymmetric distribution of information within and among eukaryotic cells. Actin-dependent transport of ASH1 mRNA in yeast represents one of the best-characterized examples of mRNP translocation. Formation of the ASH1 mRNP requires recognition of zip code elements by the RNA binding protein She2p. We determined the X-ray structure of She2p at 1.95 {\AA} resolution. She2p is a member of a previously unknown class of nucleic acid binding proteins, composed of a single globular domain with a five α helix bundle that forms a symmetric homodimer. After demonstrating potent, dimer-dependent RNA binding in vitro, we mapped the RNA binding surface of She2p to a basic helical hairpin in vitro and in vivo and present a mechanism for mRNA-dependent initiation of ASH1 mRNP complex assembly.",
author = "Dierk Niessing and Stefan H{\"u}ttelmaier and Daniel Zenklusen and Singer, {Robert H.} and Burley, {Stephen K.}",
note = "Funding Information: Use of the Advanced Photon Source was supported by the U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences, under Contract No. W-31-109-Eng-38. Use of the SGX Collaborative Access Team (SGX-CAT) beamline facilities at Sector 31 of the Advanced Photon Source was provided by Structural GenomiX, Inc., which constructed and operates the facility. We are grateful to Dr. J.B. Bonanno for technical support and advice during data analyses and structure determination; to Xiuhua Meng for excellent support with filter binding experiments; to Dr. A.K. Padyana for help during structure determination; to Dr. S. Wasserman for assistance with X-ray diffraction data collection; to Dr. Brian Noland for assistance with Circular Dichroism measurements; and to K. Bain, M. Buchanan, D. Phanstiel, Dr. X. Gao, M. Maletich, M. Riedy, and Dr. X. Zhao for technical support. We also thank Drs. S. Antonysamy, R.C. Deo, C. Groft, C. Kissinger, H.A. Lewis, G. Louie, J. Marcotrigiano, A.K. Padyana, F. Park, and X. Zhao for many useful discussions. We are thankful to J. Kosh and Dr. C. Stamper at Keck Biophysics Facility of Northwestern University (IL) and Dr. B. Demeler at The University of Texas Health Science Center at San Antonio (TX) for help with analytical ultracentrifugation. D.N. was supported by a long-term fellowship of the Human Frontiers Science Program (HFSP) and an “Otto-Hahn-Medaille” fellowship of the Max-Planck Society. S.K.B. was an investigator in the Howard Hughes Medical Institute. This work was supported by NIGMS grant GM61262 (S.K.B.) and NIGMS grant GM57071 (R.H.S.). ",
year = "2004",
month = nov,
day = "12",
doi = "10.1016/j.cell.2004.10.018",
language = "English (US)",
volume = "119",
pages = "491--502",
journal = "Cell",
issn = "0092-8674",
publisher = "Cell Press",
number = "4",
}